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1qun
From Proteopedia
(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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| - | [[Image:1qun.gif|left|200px]]<br /><applet load="1qun" size=" | + | [[Image:1qun.gif|left|200px]]<br /><applet load="1qun" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qun, resolution 2.8Å" /> | caption="1qun, resolution 2.8Å" /> | ||
'''X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM UROPATHOGENIC E.COLI'''<br /> | '''X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM UROPATHOGENIC E.COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Type 1 pili-adhesive fibers expressed in most members of the | + | 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== | ==About this Structure== | ||
| - | 1QUN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1QUN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Choudhury, D.]] | [[Category: Choudhury, D.]] | ||
| - | [[Category: Hultgren, S | + | [[Category: Hultgren, S J.]] |
[[Category: Knight, S.]] | [[Category: Knight, S.]] | ||
[[Category: Langerman, S.]] | [[Category: Langerman, S.]] | ||
| Line 22: | Line 22: | ||
[[Category: chaperone adhesin donor strand complementation]] | [[Category: chaperone adhesin donor strand complementation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:56 2008'' |
Revision as of 12:43, 21 February 2008
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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 Thu Feb 21 14:43:56 2008
