M. A. Fischbach and C. T. Walsh, Antibiotics for Emerging Pathogens, Science, vol.325, issue.5944, pp.1089-1093, 2009.
DOI : 10.1126/science.1176667

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2802854

M. Jassal and W. R. Bishai, Extensively drug-resistant tuberculosis, The Lancet Infectious Diseases, vol.9, issue.1, pp.19-30, 2009.
DOI : 10.1016/S1473-3099(08)70260-3

Y. L. Janin, Antituberculosis drugs: Ten years of research, Bioorganic & Medicinal Chemistry, vol.15, issue.7, pp.2479-2513, 2007.
DOI : 10.1016/j.bmc.2007.01.030

URL : https://hal.archives-ouvertes.fr/pasteur-00166358

E. C. Rivers and R. L. Mancera, New anti-tuberculosis drugs in clinical trials with novel mechanisms of action, Drug Discovery Today, vol.13, issue.23-24, pp.1090-1098, 2008.
DOI : 10.1016/j.drudis.2008.09.004

J. C. Sacchettini, E. J. Rubin, and J. S. Freundlich, Drugs versus bugs: in pursuit of the persistent predator Mycobacterium tuberculosis, Nature Reviews Microbiology, vol.23, issue.1, pp.41-52, 2008.
DOI : 10.1038/nrmicro1816

K. Mdluli and M. Spigelman, Novel targets for tuberculosis drug discovery, Current Opinion in Pharmacology, vol.6, issue.5, pp.459-467, 2006.
DOI : 10.1016/j.coph.2006.06.004

Y. Zhang, THE MAGIC BULLETS AND TUBERCULOSIS DRUG TARGETS, Annual Review of Pharmacology and Toxicology, vol.45, issue.1, pp.529-564, 2005.
DOI : 10.1146/annurev.pharmtox.45.120403.100120

Y. Zhang, K. Post-martens, and S. Denkin, New drug candidates and therapeutic targets for tuberculosis therapy, Drug Discovery Today, vol.11, issue.1-2, pp.21-27, 2006.
DOI : 10.1016/S1359-6446(05)03626-3

T. R. Ioerger and J. C. Sacchettini, Structural genomics approach to drug discovery for Mycobacterium tuberculosis, Current Opinion in Microbiology, vol.12, issue.3, pp.318-325, 2009.
DOI : 10.1016/j.mib.2009.04.006

M. G. Rossmann, D. Moras, and K. W. Olsen, Chemical and biological evolution of a nucleotide-binding protein, Nature, vol.243, issue.5463, pp.194-199, 1974.
DOI : 10.1038/250194a0

M. Saraste, P. R. Sibbald, and A. Wittinghofer, The P-loop ??? a common motif in ATP- and GTP-binding proteins, Trends in Biochemical Sciences, vol.15, issue.11, pp.430-434, 1990.
DOI : 10.1016/0968-0004(90)90281-F

G. E. Schulz, Structural and Functional Relationships in the Adenylate Kinase Family, Cold Spring Harbor Symposia on Quantitative Biology, vol.52, issue.0, pp.429-439, 1987.
DOI : 10.1101/SQB.1987.052.01.050

C. Vonrhein, G. J. Schlauderer, and G. E. Schulz, Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases, Structure, vol.3, issue.5, pp.483-490, 1995.
DOI : 10.1016/S0969-2126(01)00181-2

K. Fukami-kobayashi, M. Nosaka, A. Nakazawa, . Go?, and M. Go?, Ancient divergence of long and short isoforms of adenylate kinase molecular evolution of the nucleoside monophosphate kinase family, FEBS Letters, vol.268, issue.3, pp.214-220, 1996.
DOI : 10.1016/0014-5793(96)00367-5

P. Briozzo, B. Golinelli-pimpaneau, A. Gilles, J. Gaucher, S. Burlacu-miron et al., Structures of Escherichia coli CMP kinase alone and in complex with CDP: a new fold of the nucleoside monophosphate binding domain and insights into cytosine nucleotide specificity, Structure, vol.6, issue.12, pp.1517-1527, 1998.
DOI : 10.1016/S0969-2126(98)00150-6

N. Bucurenci, H. Sakamoto, P. Briozzo, N. Palibroda, L. Serina et al., CMP Kinase from Escherichia coli Is Structurally Related to Other Nucleoside Monophosphate Kinases, Journal of Biological Chemistry, vol.271, issue.5, pp.2856-2862, 1996.
DOI : 10.1074/jbc.271.5.2856

P. Coggill, R. D. Finn, and A. Bateman, Identifying Protein Domains with the Pfam Database, Curr. Protoc. Bioinformatics, vol.5, issue.2, p.5, 2008.
DOI : 10.1002/0471250953.bi0205s23

L. Serina, C. Blondin, E. Krin, O. Sismeiro, A. Danchin et al., Escherichia coli UMP kinase, a Member of the Aspartokinase Family, Is a Hexamer Regulated by Guanine Nucleotides and UTP, Biochemistry, vol.34, issue.15, pp.5066-5074, 1995.
DOI : 10.1021/bi00015a018

G. Labesse, N. Bucurenci, D. Douguet, H. Sakamoto, S. Landais et al., Comparative modelling and immunochemical reactivity of Escherichia coli UMP kinase, Biochemical and Biophysical Research Communications, vol.294, issue.1, pp.173-179, 2002.
DOI : 10.1016/S0006-291X(02)00450-3

P. Briozzo, C. Evrin, P. Meyer, L. Assairi, N. Joly et al., UMP Kinase Differs from That of Other Nucleoside Monophosphate Kinases and Sheds New Light on Enzyme Regulation, Journal of Biological Chemistry, vol.280, issue.27, pp.25533-25540, 2005.
DOI : 10.1074/jbc.M501849200

C. Marco-marin, F. Gil-ortiz, and V. Rubio, The Crystal Structure of Pyrococcus furiosus UMP Kinase Provides Insight into Catalysis and Regulation in Microbial Pyrimidine Nucleotide Biosynthesis, Journal of Molecular Biology, vol.352, issue.2, pp.438-454, 2005.
DOI : 10.1016/j.jmb.2005.07.045

J. Jang, J. Becq, B. Gicquel, P. Deschavanne, and O. Neyrolles, Horizontally acquired genomic islands in the tubercle bacilli, Trends in Microbiology, vol.16, issue.7, pp.303-308, 2008.
DOI : 10.1016/j.tim.2008.04.005

R. Brosch, S. V. Gordon, T. Garnier, K. Eiglmeier, W. Frigui et al., Genome plasticity of BCG and impact on vaccine efficacy, Proc. Natl Acad. Sci. USA, pp.5596-5601, 2007.
DOI : 10.1073/pnas.0700869104

S. T. Cole, R. Brosch, J. Parkhill, T. Garnier, C. Churcher et al., Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence, Nature, vol.25, issue.6685, pp.537-544, 1998.
DOI : 10.1038/31159

S. T. Cole, K. Eiglmeier, J. Parkhill, K. D. James, N. R. Thomson et al., Massive gene decay in the leprosy bacillus, Nature, vol.409, issue.6823, pp.1007-1011, 2001.
DOI : 10.1038/35059006

T. Garnier, K. Eiglmeier, J. C. Camus, N. Medina, H. Mansoor et al., The complete genome sequence of Mycobacterium bovis, Proc. Natl Acad. Sci. USA, pp.7877-7882, 2003.
DOI : 10.1073/pnas.1130426100

H. Munier-lehmann, S. Burlacu-miron, C. T. Craescu, H. H. Mantsch, and C. P. Schultz, A new subfamily of short bacterial adenylate kinases with the Mycobacterium tuberculosis enzyme as a model: A predictive and experimental study, Proteins: Structure, Function, and Genetics, vol.36, issue.2, pp.238-248, 1999.
DOI : 10.1002/(SICI)1097-0134(19990801)36:2<238::AID-PROT9>3.3.CO;2-B

URL : https://hal.archives-ouvertes.fr/pasteur-00167076

S. Miron, H. Munier-lehmann, and C. T. Craescu, 1 H, 13 C and 15 N resonance assignment and secondary structure of Mycobacterium tuberculosis adenylate kinase, Journal of Biomolecular NMR, vol.19, issue.1, pp.89-90, 2001.
DOI : 10.1023/A:1008392515781

URL : https://hal.archives-ouvertes.fr/pasteur-00167071

G. Hible, P. Christova, L. Renault, E. Seclaman, A. Thompson et al., Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase, Proteins: Structure, Function, and Bioinformatics, vol.3, issue.9, pp.489-500, 2006.
DOI : 10.1002/prot.20662

URL : https://hal.archives-ouvertes.fr/pasteur-00166951

H. Munier-lehmann, A. Chaffotte, S. Pochet, and G. Labesse, Thymidylate kinase of Mycobacterium tuberculosis: A chimera sharing properties common to eukaryotic and bacterial enzymes, Protein Science, vol.13, issue.6, pp.1195-1205, 2001.
DOI : 10.1110/ps.45701

URL : https://hal.archives-ouvertes.fr/pasteur-00167069

S. Pochet, L. Dugue, D. Douguet, G. Labesse, and H. Munier-lehmann, Nucleoside Analogues as Inhibitors of Thymidylate Kinases: Possible Therapeutic Applications, ChemBioChem, vol.265, issue.1, pp.108-110, 2002.
DOI : 10.1002/1439-7633(20020104)3:1<108::AID-CBIC108>3.0.CO;2-B

URL : https://hal.archives-ouvertes.fr/pasteur-00166196

S. Pochet, . Dugue´, L. Dugue´, G. Labesse, M. Delepierre et al., Comparative Study of Purine and Pyrimidine Nucleoside Analogues Acting on the Thymidylate Kinases of Mycobacterium tuberculosis and of Humans, ChemBioChem, vol.4, issue.8, pp.742-747, 2003.
DOI : 10.1002/cbic.200300608

URL : https://hal.archives-ouvertes.fr/pasteur-00165348

V. Vanheusden, H. Munier-lehmann, M. Froeyen, R. Busson, J. Rozenski et al., Thymidine Monophosphate Kinase, Journal of Medicinal Chemistry, vol.47, issue.25, pp.6187-6194, 2004.
DOI : 10.1021/jm040847w

URL : https://hal.archives-ouvertes.fr/pasteur-00166206

I. Van-daele, H. Munier-lehmann, M. Froeyen, J. Balzarini, and S. V. Calenbergh, Rational Design of 5???-Thiourea-Substituted ??-Thymidine Analogues as Thymidine Monophosphate Kinase Inhibitors Capable of Inhibiting Mycobacterial Growth, Journal of Medicinal Chemistry, vol.50, issue.22, pp.5281-5292, 2007.
DOI : 10.1021/jm0706158

URL : https://hal.archives-ouvertes.fr/hal-01197105

O. Familiar, H. Munier-lehmann, A. Negri, F. Gago, D. Douguet et al., Thymidylate Kinase, ChemMedChem, vol.23, issue.7, pp.1083-1093, 2008.
DOI : 10.1002/cmdc.200800060

URL : https://hal.archives-ouvertes.fr/pasteur-00316018

D. Douguet, H. Munier-lehmann, G. Labesse, and S. Pochet, LEA3D: A Computer-Aided Ligand Design for Structure-Based Drug Design, Journal of Medicinal Chemistry, vol.48, issue.7, pp.2457-2468, 2005.
DOI : 10.1021/jm0492296

URL : https://hal.archives-ouvertes.fr/pasteur-00166207

C. Gasse, D. Douguet, V. Huteau, G. Marchal, H. Munier-lehmann et al., Substituted benzyl-pyrimidines targeting thymidine monophosphate kinase of Mycobacterium tuberculosis: Synthesis and in vitro anti-mycobacterial activity, Bioorganic & Medicinal Chemistry, vol.16, issue.11, pp.6075-6085, 2008.
DOI : 10.1016/j.bmc.2008.04.045

URL : https://hal.archives-ouvertes.fr/pasteur-00307723

C. Thum, C. Z. Schneider, M. S. Palma, D. S. Santos, and L. A. Basso, The Rv1712 Locus from Mycobacterium tuberculosis H37Rv Codes for a Functional CMP Kinase That Preferentially Phosphorylates dCMP, Journal of Bacteriology, vol.191, issue.8, pp.2884-2887, 2009.
DOI : 10.1128/JB.01337-08

E. A. Raleigh, N. E. Murray, H. Revel, R. M. Blumenthal, D. Westaway et al., McrA and McrB restriction phenotypes of some E. coli strains and implications for gene cloning. [erratum appears in, Nucleic Acids Res. Nucleic Acids Res, vol.3612, issue.16, pp.1563-1575, 1988.

H. Munier, A. Gilles, P. Glaser, E. Krin, A. Danchin et al., Isolation and characterization of catalytic and calmodulin-binding domains of Bordetella pertussis adenylate cyclase, European Journal of Biochemistry, vol.215, issue.2, pp.469-474, 1991.
DOI : 10.1016/0968-0004(90)90177-D

URL : https://hal.archives-ouvertes.fr/pasteur-00167100

J. Sambrook, E. F. Fritsch, and T. Maniatis, Molecular Cloning: A Laboratory Manual, 1989.

V. Picard and S. C. Bock, Rapid and Efficient One-Tube PCR-Based Mutagenesis Method, Methods Mol. Biol, vol.67, pp.183-188, 1997.
DOI : 10.1385/0-89603-483-6:183

C. Blondin, L. Serina, L. Wiesmuïler, A. Gilles, and O. Ba?rzuba?rzu, Improved spectrophotometric assay of nucleoside, Nucleic Acids Research, vol.39, issue.8, p.3471, 1994.

I. At and . Pasteur, nar.oxfordjournals.org Downloaded from monophosphate kinase activity using the pyruvate kinase/lactate dehydrogenase coupling system, Anal. Biochem, vol.220, pp.219-221, 2011.

C. Evrin, M. Straut, N. Slavova-azmanova, N. Bucurenci, A. Onu et al., Regulatory Mechanisms Differ in UMP Kinases from Gram-negative and Gram-positive Bacteria, Journal of Biological Chemistry, vol.282, issue.10, pp.7242-7253, 2007.
DOI : 10.1074/jbc.M606963200

A. A. Zamyatnin, Amino Acid, Peptide, and Protein Volume in Solution, Annual Review of Biophysics and Bioengineering, vol.13, issue.1, pp.145-165, 1984.
DOI : 10.1146/annurev.bb.13.060184.001045

V. Catherinot and G. Labesse, ViTO: tool for refinement of protein sequence-structure alignments, Bioinformatics, vol.20, issue.18, pp.3694-3696, 2004.
DOI : 10.1093/bioinformatics/bth429

A. A. Canutescu, A. A. Shelenkov, R. L. Dunbrack, and . Jr, A graph-theory algorithm for rapid protein side-chain prediction, Protein Science, vol.311, issue.9, 2001.
DOI : 10.1110/ps.03154503

A. Sali and T. L. Blundell, Comparative Protein Modelling by Satisfaction of Spatial Restraints, Journal of Molecular Biology, vol.234, issue.3, pp.779-815, 1993.
DOI : 10.1006/jmbi.1993.1626

J. L. Pons and G. Labesse, @TOME-2: a new pipeline for comparative modeling of protein-ligand complexes, Nucleic Acids Research, vol.37, issue.Web Server, pp.485-491, 2009.
DOI : 10.1093/nar/gkp368

C. Computational-project and N. , The CCP4 suite: programs for protein crystallography, Acta Crystallogr, 1994.

P. Emsley and K. Cowtan, : model-building tools for molecular graphics, Acta Crystallographica Section D Biological Crystallography, vol.60, issue.12, pp.2126-2132, 2004.
DOI : 10.1107/S0907444904019158

M. D. Winn, M. N. Isupov, and G. N. Murshudov, Use of TLS parameters to model anisotropic displacements in macromolecular refinement, Acta Crystallographica Section D Biological Crystallography, vol.57, issue.1, pp.122-133, 2001.
DOI : 10.1107/S0907444900014736

P. V. Konarev, V. V. Volkov, A. V. Sokolova, M. H. Koch, and D. I. Svergun, : a Windows PC-based system for small-angle scattering data analysis, Journal of Applied Crystallography, vol.36, issue.5, pp.1277-1282, 2003.
DOI : 10.1107/S0021889803012779

D. I. Svergun, Determination of the regularization parameter in indirect-transform methods using perceptual criteria, Journal of Applied Crystallography, vol.25, issue.4, pp.495-503, 1992.
DOI : 10.1107/S0021889892001663

M. M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Analytical Biochemistry, vol.72, issue.1-2, pp.248-254, 1976.
DOI : 10.1016/0003-2697(76)90527-3

U. K. Laemmli, Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4, Nature, vol.244, issue.5259, pp.680-685, 1970.
DOI : 10.1038/227680a0

F. Fassy, O. Krebs, M. Lowinski, P. Ferrari, J. Winter et al., : evidence for co-operative ATP binding and allosteric regulation, Biochemical Journal, vol.384, issue.3, pp.619-627, 2004.
DOI : 10.1042/BJ20040440

C. Meier, L. G. Carter, S. Sainsbury, E. J. Mancini, R. J. Owens et al., The Crystal Structure of UMP Kinase from Bacillus anthracis (BA1797) Reveals an Allosteric Nucleotide-Binding Site, Journal of Molecular Biology, vol.381, issue.5, pp.1098-1105, 2008.
DOI : 10.1016/j.jmb.2008.06.078

C. Gagyi, N. Bucurenci, O. Sirbu, G. Labesse, M. Ionescu et al., UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal activity, European Journal of Biochemistry, vol.26, issue.15, pp.3196-3204, 2003.
DOI : 10.1093/bioinformatics/15.4.305

S. Ramon-maiques, A. Marina, F. Gil-ortiz, I. Fita, and V. Rubio, Structure of Acetylglutamate Kinase, a Key Enzyme for Arginine Biosynthesis and a Prototype for the Amino Acid Kinase Enzyme Family, during Catalysis, Structure, vol.10, issue.3, pp.329-342, 2002.
DOI : 10.1016/S0969-2126(02)00721-9

P. Meyer, C. Evrin, P. Briozzo, N. Joly, O. Barzu et al., Structural and Functional Characterization of Escherichia coli UMP Kinase in Complex with Its Allosteric Regulator GTP, Journal of Biological Chemistry, vol.283, issue.51, pp.36011-36018, 2008.
DOI : 10.1074/jbc.M802614200

J. L. Tu, K. H. Chin, A. H. Wang, and S. H. Chou, Unique GTP-Binding Pocket and Allostery of Uridylate Kinase from a Gram-Negative Phytopathogenic Bacterium, Journal of Molecular Biology, vol.385, issue.4, pp.1113-1126, 2009.
DOI : 10.1016/j.jmb.2008.11.030

N. Bucurenci, L. Serina, C. Zaharia, S. Landais, A. Danchin et al., Mutational analysis of UMP kinase from Escherichia coli, J. Bacteriol, vol.180, pp.473-477, 1998.

S. Proshkin, A. R. Rahmouni, A. Mironov, and E. Nudler, Cooperation Between Translating Ribosomes and RNA Polymerase in Transcription Elongation, Science, vol.328, issue.5977, pp.504-508, 2010.
DOI : 10.1126/science.1184939

L. Egeblad-welin, M. Welin, L. Wang, and S. Eriksson, Structural and functional investigations of Ureaplasma parvum UMP kinase - a potential antibacterial drug target, FEBS Journal, vol.200, issue.24, pp.6403-6414, 2007.
DOI : 10.1111/j.1742-4658.2007.06157.x

J. Monod, J. Wyman, and J. P. Changeux, On the nature of allosteric transitions: A plausible model, Journal of Molecular Biology, vol.12, issue.1, pp.88-118, 1965.
DOI : 10.1016/S0022-2836(65)80285-6

D. Kern and E. R. Zuiderweg, The role of dynamics in allosteric regulation, Current Opinion in Structural Biology, vol.13, issue.6, pp.748-757, 2003.
DOI : 10.1016/j.sbi.2003.10.008

E. Marcos, R. Crehuet, and I. Bahar, On the Conservation of the Slow Conformational Dynamics within the Amino Acid Kinase Family: NAGK the Paradigm, PLoS Computational Biology, vol.14, issue.4, 2010.
DOI : 10.1371/journal.pcbi.1000738.s003