3fhk
From Proteopedia
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- | [[ | + | ==Crystal structure of APC1446, B.subtilis YphP disulfide isomerase== |
+ | <StructureSection load='3fhk' size='340' side='right' caption='[[3fhk]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3fhk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FHK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FHK FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU21860, yphP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fhk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fhk RCSB], [http://www.ebi.ac.uk/pdbsum/3fhk PDBsum], [http://www.topsan.org/Proteins/ISFI/3fhk TOPSAN]</span></td></tr> | ||
+ | </table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/3fhk_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The DUF1094 family contains over 100 bacterial proteins, all containing a conserved CXC motif, with unknown function. We solved the crystal structure of the Bacillus subtilis representative, the product of the yphP gene. The protein shows remarkable structural similarity to thioredoxins, with a canonical alphabetaalphabetaalphabetabetaalpha topology, despite low amino acid sequence identity to thioredoxin. The CXC motif is found in the loop immediately downstream of the first beta-strand, in a location equivalent to the CXXC motif of thioredoxins, with the first Cys occupying a position equivalent to the first Cys in canonical thioredoxin. The experimentally determined reduction potential of YphP is E degrees ' = -130 mV, significantly higher than that of thioredoxin and consistent with disulfide isomerase activity. Functional assays confirmed that the protein displays a level of isomerase activity that might be biologically significant. We propose a mechanism by which the members of this family catalyze isomerization using the CXC catalytic site. | ||
- | + | Structure and Function of Bacillus subtilis YphP, a Prokaryotic Disulfide Isomerase with a CXC Catalytic Motif (,).,Derewenda U, Boczek T, Gorres KL, Yu M, Hung LW, Cooper D, Joachimiak A, Raines RT, Derewenda ZS Biochemistry. 2009 Aug 21. PMID:19653655<ref>PMID:19653655</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | ||
- | == | + | |
- | < | + | |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
- | [[Category: Boczek, T | + | [[Category: Boczek, T]] |
- | [[Category: Cooper, D R | + | [[Category: Cooper, D R]] |
- | [[Category: Derewenda, U | + | [[Category: Derewenda, U]] |
- | [[Category: Derewenda, Z S | + | [[Category: Derewenda, Z S]] |
- | [[Category: Hung, L | + | [[Category: Hung, L]] |
- | [[Category: ISFI, Integrated Center for Structure and Function Innovation | + | [[Category: ISFI, Integrated Center for Structure and Function Innovation]] |
- | [[Category: Yu, M | + | [[Category: Yu, M]] |
[[Category: Cxc motif]] | [[Category: Cxc motif]] | ||
[[Category: Disulfide isomerase]] | [[Category: Disulfide isomerase]] | ||
[[Category: Integrated center for structure and function innovation]] | [[Category: Integrated center for structure and function innovation]] | ||
[[Category: Isfi]] | [[Category: Isfi]] | ||
- | [[Category: Protein structure initiative | + | [[Category: PSI, Protein structure initiative]] |
- | + | ||
[[Category: Ser]] | [[Category: Ser]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] |
Revision as of 08:45, 26 November 2014
Crystal structure of APC1446, B.subtilis YphP disulfide isomerase
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Categories: Bacillus subtilis | Boczek, T | Cooper, D R | Derewenda, U | Derewenda, Z S | Hung, L | ISFI, Integrated Center for Structure and Function Innovation | Yu, M | Cxc motif | Disulfide isomerase | Integrated center for structure and function innovation | Isfi | PSI, Protein structure initiative | Ser | Structural genomic | Surface entropy reduction | Thioredoxin superfamily | Unknown function