3fhk: Difference between revisions

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-'''Unreleased structure'''
-The entry 3fhk is ON HOLD
+==Crystal structure of APC1446, B.subtilis YphP disulfide isomerase==
+<StructureSection load='3fhk' size='340' side='right'caption='[[3fhk]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-Authors: Derewenda, U., Boczek, T., Cooper, D.R., Yu, M., Hung, L., Derewenda, Z.S., Integrated Center for Structure and Function Innovation (ISFI)
+== Structural highlights ==
+<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>
-Description: Crystal structure of APC1446, B.subtilis YphP disulfide isomerase
+</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 21 10:38:17 2009''
+<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>
+== 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 ==
+[[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/main_output.php?pdb_ID=3fhk ConSurf].
+<div style="clear:both"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Bacillus subtilis]]
+[[Category: Large Structures]]
+[[Category: Boczek T]]
+[[Category: Cooper DR]]
+[[Category: Derewenda U]]
+[[Category: Derewenda ZS]]
+[[Category: Hung L]]
+[[Category: Yu M]]