Type II secretion: from structure to function, FEMS Microbiology Letters, vol.255, issue.2, pp.175-186, 2006. ,
DOI : 10.1111/j.1574-6968.2006.00102.x
Towards a systems biology approach to study type II/IV secretion systems, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.1778, issue.9, pp.1839-1850, 2008. ,
DOI : 10.1016/j.bbamem.2008.03.011
Pilus formation and protein secretion by the same machinery in Escherichia coli, The EMBO Journal, vol.96, issue.10, pp.2221-2228, 2000. ,
DOI : 10.1093/emboj/19.10.2221
Type IV-Like Pili Formed by the Type II Secreton: Specificity, Composition, Bundling, Polar Localization, and Surface Presentation of Peptides, Journal of Bacteriology, vol.185, issue.11, pp.3416-3428, 2003. ,
DOI : 10.1128/JB.185.11.3416-3428.2003
Type II Protein Secretion in Pseudomonas aeruginosa: the Pseudopilus Is a Multifibrillar and Adhesive Structure, Journal of Bacteriology, vol.185, issue.9, pp.2749-2758, 2003. ,
DOI : 10.1128/JB.185.9.2749-2758.2003
An inner membrane platform in the type II secretion machinery of Gram-negative bacteria, EMBO reports, vol.143, issue.3, pp.244-248, 2001. ,
DOI : 10.1093/embo-reports/kve042
Type IV Pilus Structure by Cryo-Electron Microscopy and Crystallography: Implications for Pilus Assembly and Functions, Molecular Cell, vol.23, issue.5, pp.651-662, 2006. ,
DOI : 10.1016/j.molcel.2006.07.004
URL : http://doi.org/10.1016/j.molcel.2006.07.004
Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins, The EMBO Journal, vol.16, issue.11, pp.3007-3016, 1997. ,
DOI : 10.1093/emboj/16.11.3007
Structure and assembly of the pseudopilin PulG, Molecular Microbiology, vol.19, issue.3, pp.647-664, 2004. ,
DOI : 10.1111/j.1365-2958.2004.04307.x
Signal Recognition Particle-Dependent Inner Membrane Targeting of the PulG Pseudopilin Component of a Type II Secretion System, Journal of Bacteriology, vol.189, issue.5, pp.1783-1793, 2007. ,
DOI : 10.1128/JB.01230-06
URL : https://hal.archives-ouvertes.fr/hal-00138935
Multiple Interactions between Pullulanase Secreton Components Involved in Stabilization and Cytoplasmic Membrane Association of PulE, Journal of Bacteriology, vol.182, issue.8, pp.2142-2152, 2000. ,
DOI : 10.1128/JB.182.8.2142-2152.2000
Calcium Is Essential for the Major Pseudopilin in the Type 2 Secretion System, Journal of Biological Chemistry, vol.284, issue.38, pp.25466-25470, 2009. ,
DOI : 10.1074/jbc.C109.037655
Type IV Pilin Structure and Assembly, Molecular Cell, vol.11, issue.5, pp.1139-1150, 2003. ,
DOI : 10.1016/S1097-2765(03)00170-9
URL : http://doi.org/10.1016/s1097-2765(03)00170-9
Amino acid substitutions in pilin of Pseudomonas aeruginosa. Effect on leader peptide cleavage, amino-terminal methylation, and pilus assembly, 1991. ,
Towards the Identification of Type II Secretion Signals in a Nonacylated Variant of Pullulanase from Klebsiella oxytoca, Journal of Bacteriology, vol.187, issue.20, pp.7045-7055, 2005. ,
DOI : 10.1128/JB.187.20.7045-7055.2005
Vibrio cholerae Toxin-Coregulated Pilus Structure Analyzed by Hydrogen/Deuterium Exchange Mass Spectrometry, Structure, vol.16, issue.1, pp.137-148, 2008. ,
DOI : 10.1016/j.str.2007.10.027
URL : http://doi.org/10.1016/j.str.2007.10.027
Dynamic Formation and Breaking of Disulfide Bonds in Molecular Dynamics Simulations with the UNRES Force Field, Journal of Chemical Theory and Computation, vol.3, issue.4, pp.1236-1248, 2007. ,
DOI : 10.1021/ct7000842
The Advent of Near-Atomic Resolution in Single-Particle Electron Microscopy, Annual Review of Biochemistry, vol.78, issue.1, pp.723-742, 2009. ,
DOI : 10.1146/annurev.biochem.78.070507.140543
Substitutions in the N-terminal alpha helical spine of Neisseria gonorrhoeae pilin affect Type IV pilus assembly, dynamics and associated functions, Molecular Microbiology, vol.266, issue.1, 2007. ,
DOI : 10.1073/pnas.89.12.5366
Structure of the GspK???GspI???GspJ complex from the enterotoxigenic Escherichia coli type 2 secretion system, Nature Structural & Molecular Biology, vol.175, issue.5, pp.462-468, 2008. ,
DOI : 10.1107/S0907444906005270
The XcpV/GspI Pseudopilin Has a Central Role in the Assembly of a Quaternary Complex within the T2SS Pseudopilus, Journal of Biological Chemistry, vol.284, issue.50, pp.34580-34589, 2009. ,
DOI : 10.1074/jbc.M109.042366
The type II secretion arrowhead: the structure of GspI???GspJ???GspK, Nature Structural & Molecular Biology, vol.15, issue.5, 2008. ,
DOI : 10.1016/S0959-440X(00)00129-9
Structure of thePseudomonas aeruginosa XcpT pseudopilin, a major component of the type II secretion system, Journal of Structural Biology, vol.169, issue.1, pp.75-80, 2010. ,
DOI : 10.1016/j.jsb.2009.09.003
SCWRL and MolIDE: computer programs for side-chain conformation prediction and homology modeling, Nature Protocols, vol.102, issue.12, pp.1832-1847, 2008. ,
DOI : 10.1016/j.jmb.2007.10.060
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2682191
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination, Acta Crystallographica Section D Biological Crystallography, vol.54, issue.5, pp.905-921, 1998. ,
DOI : 10.1107/S0907444998003254
Protein structure calculation using ambiguous restraints. Encyclopedia of Magnetic Resonance, 2010. ,
DOI : 10.1002/9780470034590.emrstm1156
Protein molecular dynamics with the generalized born/ACE solvent model, Proteins: Structure, Function, and Genetics, vol.3, issue.2, pp.144-158, 2001. ,
DOI : 10.1002/prot.1134
Reintroducing electrostatics into protein X-ray structure refinement: bulk solvent treated as a dielectric continuum, Acta Crystallographica Section D Biological Crystallography, vol.59, issue.12, pp.2094-2103, 2003. ,
DOI : 10.1107/S090744490301833X
URL : https://hal.archives-ouvertes.fr/hal-00770916
CHARMM: A program for macromolecular energy, minimization, and dynamics calculations, Journal of Computational Chemistry, vol.I, issue.2, pp.187-217, 1983. ,
DOI : 10.1002/jcc.540040211
VMD: Visual molecular dynamics, Journal of Molecular Graphics, vol.14, issue.1, pp.33-38, 1996. ,
DOI : 10.1016/0263-7855(96)00018-5
Electrostatics of nanosystems: Application to microtubules and the ribosome, Proceedings of the National Academy of Sciences, vol.377, issue.6547, pp.10037-10041, 2001. ,
DOI : 10.1038/377309a0
Refinement of protein structures in explicit solvent, Proteins: Structure, Function, and Bioinformatics, vol.8, issue.3, pp.496-506, 2003. ,
DOI : 10.1002/prot.10299
Comparison of simple potential functions for simulating liquid water, The Journal of Chemical Physics, vol.79, issue.2, pp.926-935, 1983. ,
DOI : 10.1016/0009-2614(80)85344-9
Accurate NMR Structures Through Minimization of an Extended Hybrid Energy, Structure, vol.16, issue.9, pp.1305-1312, 2008. ,
DOI : 10.1016/j.str.2008.07.008
PROCHECK: a program to check the stereochemical quality of protein structures, Journal of Applied Crystallography, vol.26, issue.2, pp.283-291, 1993. ,
DOI : 10.1107/S0021889892009944
Reintroducing electrostatics into protein X-ray structure refinement: bulk solvent treated as a dielectric continuum, Acta Crystallographica Section D Biological Crystallography, vol.59, issue.12, pp.2094-2103, 2003. ,
DOI : 10.1107/S090744490301833X
URL : https://hal.archives-ouvertes.fr/hal-00770916
Protein-protein recognition and interaction hot spots in an antigen-antibody complex: Free energy decomposition identifies ???efficient amino acids???, Proteins: Structure, Function, and Bioinformatics, vol.101, issue.2, pp.418-434, 2007. ,
DOI : 10.1002/prot.21259
URL : https://hal.archives-ouvertes.fr/hal-00190960
Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives, Gene, vol.102, issue.1, pp.75-78, 1991. ,
DOI : 10.1016/0378-1119(91)90541-I
Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase, EMBO J, vol.6, pp.3531-3538, 1987. ,
Multiple Interactions between Pullulanase Secreton Components Involved in Stabilization and Cytoplasmic Membrane Association of PulE, Journal of Bacteriology, vol.182, issue.8, pp.2142-2152, 2000. ,
DOI : 10.1128/JB.182.8.2142-2152.2000
Modeling run of the T2S pilus Each frame represents a step in the modeling process with all of the implicit protomers represented by symmetry. Protomers are attracted toward the pilus axis, are arranged first in a left-handed helix, and then converge toward one of the right-handed helix models in the main cluster ,