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[[Image: | ==CRYSTAL STRUCTURE OF THE ORGANIC HYDROPEROXIDE RESISTANCE PROTEIN OHRB OF BACILLUS SUBTILIS== | ||
<StructureSection load='2bjo' size='340' side='right' caption='[[2bjo]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bjo]] is a 2 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=2BJO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BJO FirstGlance]. <br> | |||
</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=2bjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bjo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bjo RCSB], [http://www.ebi.ac.uk/pdbsum/2bjo PDBsum]</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/bj/2bjo_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 crystal structure of the fully oxidized form of the Bacillus subtilis organic hydroperoxide-resistance (OhrB) protein is reported at 2.1 A resolution. The electron density reveals an intact catalytic disulfide bond (Cys55-Cys119) in each of the two molecules, which are intertwined into a canonical obligate dimer. However, the stereochemistry of the disulfides is unorthodox and strained, suggesting that they are sensitive to reducing agents. A deep solvent-accessible gorge reaching Cys55 may represent the access route for the reductant. | |||
Structure of the Bacillus subtilis OhrB hydroperoxide-resistance protein in a fully oxidized state.,Cooper DR, Surendranath Y, Devedjiev Y, Bielnicki J, Derewenda ZS Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1269-73. Epub 2007, Nov 16. PMID:18084074<ref>PMID:18084074</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Organic hydroperoxide resistance protein|Organic hydroperoxide resistance protein]] | *[[Organic hydroperoxide resistance protein|Organic hydroperoxide resistance protein]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Bielnicki, J.]] | [[Category: Bielnicki, J.]] |
Revision as of 05:25, 29 September 2014
CRYSTAL STRUCTURE OF THE ORGANIC HYDROPEROXIDE RESISTANCE PROTEIN OHRB OF BACILLUS SUBTILISCRYSTAL STRUCTURE OF THE ORGANIC HYDROPEROXIDE RESISTANCE PROTEIN OHRB OF BACILLUS SUBTILIS
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the fully oxidized form of the Bacillus subtilis organic hydroperoxide-resistance (OhrB) protein is reported at 2.1 A resolution. The electron density reveals an intact catalytic disulfide bond (Cys55-Cys119) in each of the two molecules, which are intertwined into a canonical obligate dimer. However, the stereochemistry of the disulfides is unorthodox and strained, suggesting that they are sensitive to reducing agents. A deep solvent-accessible gorge reaching Cys55 may represent the access route for the reductant. Structure of the Bacillus subtilis OhrB hydroperoxide-resistance protein in a fully oxidized state.,Cooper DR, Surendranath Y, Devedjiev Y, Bielnicki J, Derewenda ZS Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1269-73. Epub 2007, Nov 16. PMID:18084074[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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