1bf8: Difference between revisions

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[[Image:1bf8.gif|left|200px]]<br /><applet load="1bf8" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1bf8.gif|left|200px]]
caption="1bf8" />
 
'''PERIPLASMIC CHAPERONE FIMC, NMR, 20 STRUCTURES'''<br />
{{Structure
|PDB= 1bf8 |SIZE=350|CAPTION= <scene name='initialview01'>1bf8</scene>
|SITE=  
|LIGAND=  
|ACTIVITY=  
|GENE=  
}}
 
'''PERIPLASMIC CHAPERONE FIMC, NMR, 20 STRUCTURES'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1BF8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1BF8 OCA].  
1BF8 is a [[Single protein]] structure of sequence 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=1BF8 OCA].  


==Reference==
==Reference==
NMR solution structure of the periplasmic chaperone FimC., Pellecchia M, Guntert P, Glockshuber R, Wuthrich K, Nat Struct Biol. 1998 Oct;5(10):885-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9783748 9783748]
NMR solution structure of the periplasmic chaperone FimC., Pellecchia M, Guntert P, Glockshuber R, Wuthrich K, Nat Struct Biol. 1998 Oct;5(10):885-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9783748 9783748]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: type-i pili]]
[[Category: type-i pili]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:38 2008''
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Revision as of 11:10, 20 March 2008

File:1bf8.gif


PDB ID 1bf8

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PERIPLASMIC CHAPERONE FIMC, NMR, 20 STRUCTURES


OverviewOverview

The NMR structure of the 205-residue periplasmic chaperone FimC is presented. This protein consists of two globular domains with immunoglobulin-like folds connected by a 15-residue linker peptide. The relative orientation of the two domains is defined by hydrophobic contacts and an interdomain salt bridge. FimC mediates the assembly of type-1 pili, which are filamentous surface organelles of uropathogenic Escherichia coli strains that enable the bacteria to attach to host cell surfaces and persist in macrophages. The availability of the NMR structure of FimC provides a new basis for rational design of drugs against infections by uropathogenic bacteria.

About this StructureAbout this Structure

1BF8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

NMR solution structure of the periplasmic chaperone FimC., Pellecchia M, Guntert P, Glockshuber R, Wuthrich K, Nat Struct Biol. 1998 Oct;5(10):885-90. PMID:9783748

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