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3GN9

Crystal structure of the major pseudopilin from the type 2 secretion system of Vibrio vulnificus

Summary for 3GN9
Entry DOI10.2210/pdb3gn9/pdb
Related1T92 3FU1 3G20
DescriptorType II secretory pathway, pseudopilin EpsG, CALCIUM ION, D-MALATE, ... (4 entities in total)
Functional Keywordsgeneral secretory pathway, major pilin, protein transport, complex, methylation
Biological sourceVibrio vulnificus
Total number of polymer chains3
Total formula weight38145.80
Authors
Korotkov, K.V.,Gray, M.D.,Kreger, A.,Turley, S.,Sandkvist, M.,Hol, W.G.J. (deposition date: 2009-03-16, release date: 2009-07-28, Last modification date: 2023-09-06)
Primary citationKorotkov, K.V.,Gray, M.D.,Kreger, A.,Turley, S.,Sandkvist, M.,Hol, W.G.
Calcium is essential for the major pseudopilin in the type 2 secretion system.
J.Biol.Chem., 284:25466-25470, 2009
Cited by
PubMed Abstract: The pseudopilus is a key feature of the type 2 secretion system (T2SS) and is made up of multiple pseudopilins that are similar in fold to the type 4 pilins. However, pilins have disulfide bridges, whereas the major pseudopilins of T2SS do not. A key question is therefore how the pseudopilins, and in particular, the most abundant major pseudopilin, GspG, obtain sufficient stability to perform their function. Crystal structures of Vibrio cholerae, Vibrio vulnificus, and enterohemorrhagic Escherichia coli (EHEC) GspG were elucidated, and all show a calcium ion bound at the same site. Conservation of the calcium ligands fully supports the suggestion that calcium ion binding by the major pseudopilin is essential for the T2SS. Functional studies of GspG with mutated calcium ion-coordinating ligands were performed to investigate this hypothesis and show that in vivo protease secretion by the T2SS is severely impaired. Taking all evidence together, this allows the conclusion that, in complete contrast to the situation in the type 4 pili system homologs, in the T2SS, the major protein component of the central pseudopilus is dependent on calcium ions for activity.
PubMed: 19640838
DOI: 10.1074/jbc.C109.037655
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.86 Å)
Structure validation

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数据于2024-10-30公开中

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