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2co7
From Proteopedia
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Revision as of 08:39, 30 October 2007
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SALMONELLA ENTERICA SAFA PILIN IN COMPLEX WITH THE SAFB CHAPERONE (TYPE II)
Overview
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 ... [(full description)]
About this Structure
2CO7 is a [Protein complex] structure of sequences from [Salmonella typhimurium] with SO4 as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism., Remaut H, Rose RJ, Hannan TJ, Hultgren SJ, Radford SE, Ashcroft AE, Waksman G, Mol Cell. 2006 Jun 23;22(6):831-42. PMID:16793551
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