1qun

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qun OCA], [http://www.ebi.ac.uk/pdbsum/1qun PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qun RCSB]</span>
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[[Category: chaperone adhesin donor strand complementation]]
[[Category: chaperone adhesin donor strand complementation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:19:18 2008''

Revision as of 20:19, 30 March 2008


PDB ID 1qun

Drag the structure with the mouse to rotate
, resolution 2.8Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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