2CO1
Salmonella enterica SafA pilin in complex with a 19-residue SafA Nte peptide (F17A mutant)
Summary for 2CO1
| Entry DOI | 10.2210/pdb2co1/pdb |
| Related | 2CNY 2CNZ 2CO2 2CO3 2CO4 2CO6 2CO7 |
| Descriptor | PUTATIVE OUTER MEMBRANE PROTEIN (3 entities in total) |
| Functional Keywords | pilus subunit, fibril protein, fold complementation |
| Biological source | SALMONELLA TYPHIMURIUM More |
| Total number of polymer chains | 2 |
| Total formula weight | 15227.92 |
| Authors | Remaut, H.,Rose, R.J.,Hannan, T.J.,Hultgren, S.J.,Radford, S.E.,Ashcroft, A.E.,Waksman, G. (deposition date: 2006-05-25, release date: 2006-06-27, Last modification date: 2024-05-01) |
| Primary citation | Remaut, H.,Rose, R.J.,Hannan, T.J.,Hultgren, S.J.,Radford, S.E.,Ashcroft, A.E.,Waksman, G. Donor-Strand Exchange in Chaperone-Assisted Pilus Assembly Proceeds Through a Concerted Beta-Strand Displacement Mechanism Mol.Cell, 22:831-, 2006 Cited by PubMed Abstract: Gram-negative pathogens commonly use the chaperone-usher pathway to assemble adhesive multisubunit fibers on their surface. In the periplasm, subunits are stabilized by a chaperone that donates a beta strand to complement the subunits' truncated immunoglobulin-like fold. Pilus assembly proceeds through a "donor-strand exchange" (DSE) mechanism whereby this complementary beta strand is replaced by the N-terminal extension (Nte) of an incoming pilus subunit. Using X-ray crystallography and real-time electrospray ionization mass spectrometry (ESI-MS), we demonstrate that DSE requires the formation of a transient ternary complex between the chaperone-subunit complex and the Nte of the next subunit to be assembled. The process is crucially dependent on an initiation site (the P5 pocket) needed to recruit the incoming Nte. The data also suggest a capping reaction displacing DSE toward product formation. These results support a zip-in-zip-out mechanism for DSE and a catalytic role for the usher, the molecular platform at which pili are assembled. PubMed: 16793551DOI: 10.1016/J.MOLCEL.2006.05.033 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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