4QTQ
Structure of a Xanthomonas Type IV Secretion System related protein
Summary for 4QTQ
Entry DOI | 10.2210/pdb4qtq/pdb |
Descriptor | XAC2610 protein, CALCIUM ION (3 entities in total) |
Functional Keywords | beta-sandwich, calcium binding motif, beta-propeller fragment, peptidoglycan hydrolase inhibitor, immunity protein xanthomonas, hydrolase inhibitor |
Biological source | Xanthomonas axonopodis pv. citri |
Total number of polymer chains | 1 |
Total formula weight | 23357.08 |
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 citation | Souza, 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: 25743609DOI: 10.1038/ncomms7453 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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