2FM9
Structure of Salmonella SipA residues 48-264
Summary for 2FM9
| Entry DOI | 10.2210/pdb2fm9/pdb |
| Descriptor | Cell invasion protein sipA (2 entities in total) |
| Functional Keywords | salmonella, type ii secretion, sipa, virulence, bacterial, cell invasion |
| Biological source | Salmonella typhimurium |
| Total number of polymer chains | 1 |
| Total formula weight | 23582.23 |
| Authors | Lilic, M.,Vujanac, M.,Stebbins, C.E. (deposition date: 2006-01-08, release date: 2006-03-21, Last modification date: 2024-02-14) |
| Primary citation | Lilic, M.,Vujanac, M.,Stebbins, C.E. A common structural motif in the binding of virulence factors to bacterial secretion chaperones. Mol.Cell, 21:653-664, 2006 Cited by PubMed Abstract: Salmonella invasion protein A (SipA) is translocated into host cells by a type III secretion system (T3SS) and comprises two regions: one domain binds its cognate type III secretion chaperone, InvB, in the bacterium to facilitate translocation, while a second domain functions in the host cell, contributing to bacterial uptake by polymerizing actin. We present here the crystal structures of the SipA chaperone binding domain (CBD) alone and in complex with InvB. The SipA CBD is found to consist of a nonglobular polypeptide as well as a large globular domain, both of which are necessary for binding to InvB. We also identify a structural motif that may direct virulence factors to their cognate chaperones in a diverse range of pathogenic bacteria. Disruption of this structural motif leads to a destabilization of several chaperone-substrate complexes from different species, as well as an impairment of secretion in Salmonella. PubMed: 16507363DOI: 10.1016/j.molcel.2006.01.026 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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