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4FTF

Structure of the Type II secretion system pilotin AspS from Vibrio cholerae

Summary for 4FTF
Entry DOI10.2210/pdb4ftf/pdb
DescriptorAlternate secretin pathway subunit S (VC395_1821, VC1703), ZINC ION, ACETATE ION, ... (4 entities in total)
Functional Keywordspilotin, lipoprotein, secretin, protein secretion, pfamb pb000779, secretin binding, outer membrane, protein transport
Biological sourceVibrio cholerae
Total number of polymer chains1
Total formula weight12633.36
Authors
Korotkov, K.V.,Evans, T.J. (deposition date: 2012-06-27, release date: 2012-11-28, Last modification date: 2024-10-30)
Primary citationDunstan, R.A.,Heinz, E.,Wijeyewickrema, L.C.,Pike, R.N.,Purcell, A.W.,Evans, T.J.,Praszkier, J.,Robins-Browne, R.M.,Strugnell, R.A.,Korotkov, K.V.,Lithgow, T.
Assembly of the Type II Secretion System such as Found in Vibrio cholerae Depends on the Novel Pilotin AspS.
Plos Pathog., 9:e1003117-e1003117, 2013
Cited by
PubMed Abstract: The Type II Secretion System (T2SS) is a molecular machine that drives the secretion of fully-folded protein substrates across the bacterial outer membrane. A key element in the machinery is the secretin: an integral, multimeric outer membrane protein that forms the secretion pore. We show that three distinct forms of T2SSs can be distinguished based on the sequence characteristics of their secretin pores. Detailed comparative analysis of two of these, the Klebsiella-type and Vibrio-type, showed them to be further distinguished by the pilotin that mediates their transport and assembly into the outer membrane. We have determined the crystal structure of the novel pilotin AspS from Vibrio cholerae, demonstrating convergent evolution wherein AspS is functionally equivalent and yet structurally unrelated to the pilotins found in Klebsiella and other bacteria. AspS binds to a specific targeting sequence in the Vibrio-type secretins, enhances the kinetics of secretin assembly, and homologs of AspS are found in all species of Vibrio as well those few strains of Escherichia and Shigella that have acquired a Vibrio-type T2SS.
PubMed: 23326233
DOI: 10.1371/journal.ppat.1003117
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.48 Å)
Structure validation

226707

數據於2024-10-30公開中

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