3fhk: Difference between revisions

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<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 [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. 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>
<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" id="ligandDat"><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 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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'>[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>
<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]]
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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/main_output.php?pdb_ID=3fhk 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>
<div class="pdbe-citations 3fhk" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Vibrio subtilis ehrenberg 1835]]
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Boczek, T]]
[[Category: Boczek T]]
[[Category: Cooper, D R]]
[[Category: Cooper DR]]
[[Category: Derewenda, U]]
[[Category: Derewenda U]]
[[Category: Derewenda, Z S]]
[[Category: Derewenda ZS]]
[[Category: Hung, L]]
[[Category: Hung L]]
[[Category: ISFI, Integrated Center for Structure and Function Innovation]]
[[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]]

Latest revision as of 12:49, 21 February 2024

Crystal structure of APC1446, B.subtilis YphP disulfide isomeraseCrystal structure of APC1446, B.subtilis YphP disulfide isomerase

Structural highlights

3fhk is a 4 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

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).[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Derewenda U, Boczek T, Gorres KL, Yu M, Hung LW, Cooper D, Joachimiak A, Raines RT, Derewenda ZS. Structure and Function of Bacillus subtilis YphP, a Prokaryotic Disulfide Isomerase with a CXC Catalytic Motif (,). Biochemistry. 2009 Aug 21. PMID:19653655 doi:10.1021/bi900437z
  2. ↑ Gaballa A, Chi BK, Roberts AA, Becher D, Hamilton CJ, Antelmann H, Helmann JD. Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and BrxB(YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and MetE. Antioxid Redox Signal. 2014 Jul 20;21(3):357-67. PMID:24313874 doi:10.1089/ars.2013.5327

3fhk, resolution 2.30Å

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