1bf8

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[[Image:1bf8.png|left|200px]]
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==PERIPLASMIC CHAPERONE FIMC, NMR, 20 STRUCTURES==
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<StructureSection load='1bf8' size='340' side='right' caption='[[1bf8]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bf8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BF8 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bf8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bf8 RCSB], [http://www.ebi.ac.uk/pdbsum/1bf8 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/1bf8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_1bf8| PDB=1bf8 | SCENE= }}
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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<ref>PMID:9783748</ref>
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===PERIPLASMIC CHAPERONE FIMC, NMR, 20 STRUCTURES===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_9783748}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1bf8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BF8 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:009783748</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Glockshuber, R.]]
[[Category: Glockshuber, R.]]

Revision as of 03:26, 7 August 2014

PERIPLASMIC CHAPERONE FIMC, NMR, 20 STRUCTURES

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