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1qun
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(New page: 200px<br /><applet load="1qun" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qun, resolution 2.8Å" /> '''X-RAY STRUCTURE OF TH...)
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Revision as of 22:53, 20 November 2007
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X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM UROPATHOGENIC E.COLI
Overview
Type 1 pili-adhesive fibers expressed in most members of the, Enterobacteriaceae family-mediate binding to mannose receptors on host, cells through the FimH adhesin. Pilus biogenesis proceeds by way of the, chaperone/usher pathway. The x-ray structure of the FimC-FimH, chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5, angstrom resolution reveals the basis for carbohydrate recognition and for, pilus assembly. The carboxyl-terminal pilin domain of FimH has an, immunoglobulin-like fold, except that the seventh strand is missing, leaving part of the hydrophobic core exposed. A donor strand, complementation mechanism in which the chaperone donates a strand to, complete the pilin domain explains the basis for both chaperone function, and pilus biogenesis.
About this Structure
1QUN is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli., Choudhury D, Thompson A, Stojanoff V, Langermann S, Pinkner J, Hultgren SJ, Knight SD, Science. 1999 Aug 13;285(5430):1061-6. PMID:10446051
Page seeded by OCA on Wed Nov 21 01:00:17 2007
