3fhk: Difference between revisions

Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(4 intermediate revisions by the same user not shown)
Line 1: Line 1:
==Crystal structure of APC1446, B.subtilis YphP disulfide isomerase==
==Crystal structure of APC1446, B.subtilis YphP disulfide isomerase==
<StructureSection load='3fhk' size='340' side='right' caption='[[3fhk]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3fhk' size='340' side='right'caption='[[3fhk]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== 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>
<table><tr><td colspan='2'>[[3fhk]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fhk OCA], [https://pdbe.org/3fhk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fhk RCSB], [https://www.ebi.ac.uk/pdbsum/3fhk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fhk ProSAT], [https://www.topsan.org/Proteins/ISFI/3fhk TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BRXA_BACSU BRXA_BACSU] S-bacillithiolation is the formation of mixed disulfide bonds between protein thiols and the general thiol reductant bacillithiol (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH) in Firmicutes. This protein is a dithiol bacilliredoxin, which debacillithiolates (removes BSH) the S-bacillithiolated OhrR (OhrR-SSB) in vitro and in vivo NaOCl-generated S-bacillithiolated MetE (MetE-SSB). Involved in maintaining redox homeostasis in response to disulfide stress conditions (PubMed:24313874). Has a redox potential of -130 mV. Displays weak protein disulfide isomerase activity in vitro (PubMed:19653655).<ref>PMID:19653655</ref> <ref>PMID:24313874</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/3fhk_consurf.spt"</scriptWhenChecked>
     <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>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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].
</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/main_output.php?pdb_ID=3fhk ConSurf].
<div style="clear:both"></div>
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
== References ==
<references/>
<references/>
Line 30: Line 25:
</StructureSection>
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Boczek, T]]
[[Category: Large Structures]]
[[Category: Cooper, D R]]
[[Category: Boczek T]]
[[Category: Derewenda, U]]
[[Category: Cooper DR]]
[[Category: Derewenda, Z S]]
[[Category: Derewenda U]]
[[Category: Hung, L]]
[[Category: Derewenda ZS]]
[[Category: ISFI, Integrated Center for Structure and Function Innovation]]
[[Category: Hung L]]
[[Category: Yu, M]]
[[Category: Yu M]]
[[Category: Cxc motif]]
[[Category: Disulfide isomerase]]
[[Category: Integrated center for structure and function innovation]]
[[Category: Isfi]]
[[Category: PSI, Protein structure initiative]]
[[Category: Ser]]
[[Category: Structural genomic]]
[[Category: Surface entropy reduction]]
[[Category: Thioredoxin superfamily]]
[[Category: Unknown function]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/w/3fhk"