1qun: Difference between revisions

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[[Image:1qun.gif|left|200px]]
{{Seed}}
[[Image:1qun.png|left|200px]]


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{{STRUCTURE_1qun|  PDB=1qun  |  SCENE=  }}  
{{STRUCTURE_1qun|  PDB=1qun  |  SCENE=  }}  


'''X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM UROPATHOGENIC E.COLI'''
===X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM UROPATHOGENIC E.COLI===




==Overview==
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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.
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{{ABSTRACT_PUBMED_10446051}}


==About this Structure==
==About this Structure==
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[[Category: Thompson, A.]]
[[Category: Thompson, A.]]
[[Category: Chaperone adhesin donor strand complementation]]
[[Category: Chaperone adhesin donor strand complementation]]
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Revision as of 02:00, 28 July 2008

File:1qun.png

Template:STRUCTURE 1qun

X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM UROPATHOGENIC E.COLI

Template:ABSTRACT PUBMED 10446051

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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