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4QTQ

Structure of a Xanthomonas Type IV Secretion System related protein

Summary for 4QTQ
Entry DOI10.2210/pdb4qtq/pdb
DescriptorXAC2610 protein, CALCIUM ION (3 entities in total)
Functional Keywordsbeta-sandwich, calcium binding motif, beta-propeller fragment, peptidoglycan hydrolase inhibitor, immunity protein xanthomonas, hydrolase inhibitor
Biological sourceXanthomonas axonopodis pv. citri
Total number of polymer chains1
Total formula weight23357.08
Authors
Souza, D.P.,Guzzo, C.R.,Farah, C.S. (deposition date: 2014-07-08, release date: 2015-06-17, Last modification date: 2024-10-09)
Primary citationSouza, D.P.,Oka, G.U.,Alvarez-Martinez, C.E.,Bisson-Filho, A.W.,Dunger, G.,Hobeika, L.,Cavalcante, N.S.,Alegria, M.C.,Barbosa, L.R.,Salinas, R.K.,Guzzo, C.R.,Farah, C.S.
Bacterial killing via a type IV secretion system.
Nat Commun, 6:6453-6453, 2015
Cited by
PubMed Abstract: Type IV secretion systems (T4SSs) are multiprotein complexes that transport effector proteins and protein-DNA complexes through bacterial membranes to the extracellular milieu or directly into the cytoplasm of other cells. Many bacteria of the family Xanthomonadaceae, which occupy diverse environmental niches, carry a T4SS with unknown function but with several characteristics that distinguishes it from other T4SSs. Here we show that the Xanthomonas citri T4SS provides these cells the capacity to kill other Gram-negative bacterial species in a contact-dependent manner. The secretion of one type IV bacterial effector protein is shown to require a conserved C-terminal domain and its bacteriolytic activity is neutralized by a cognate immunity protein whose 3D structure is similar to peptidoglycan hydrolase inhibitors. This is the first demonstration of the involvement of a T4SS in bacterial killing and points to this special class of T4SS as a mediator of both antagonistic and cooperative interbacterial interactions.
PubMed: 25743609
DOI: 10.1038/ncomms7453
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

229380

건을2024-12-25부터공개중

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