View source for 5doq


==The structure of bd oxidase from Geobacillus thermodenitrificans==
<StructureSection load='5doq' size='340' side='right' caption='[[5doq]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5doq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_sp._pa-3 Geobacillus sp. pa-3] and [http://en.wikipedia.org/wiki/Geobacillus_thermodenitrificans_(strain_ng80-2) Geobacillus thermodenitrificans (strain ng80-2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DOQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DOQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HDD:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE'>HDD</scene>, <scene name='pdbligand=HEB:HEME+B/C'>HEB</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=5doq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5doq OCA], [http://pdbe.org/5doq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5doq RCSB], [http://www.ebi.ac.uk/pdbsum/5doq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5doq ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The cytochrome bd oxidases are terminal oxidases that are present in bacteria and archaea. They reduce molecular oxygen (dioxygen) to water, avoiding the production of reactive oxygen species. In addition to their contribution to the proton motive force, they mediate viability under oxygen-related stress conditions and confer tolerance to nitric oxide, thus contributing to the virulence of pathogenic bacteria. Here we present the atomic structure of the bd oxidase from Geobacillus thermodenitrificans, revealing a pseudosymmetrical subunit fold. The arrangement and order of the heme cofactors support the conclusions from spectroscopic measurements that the cleavage of the dioxygen bond may be mechanistically similar to that in the heme-copper-containing oxidases, even though the structures are completely different.

Structure of a bd oxidase indicates similar mechanisms for membrane-integrated oxygen reductases.,Safarian S, Rajendran C, Muller H, Preu J, Langer JD, Ovchinnikov S, Hirose T, Kusumoto T, Sakamoto J, Michel H Science. 2016 Apr 29;352(6285):583-6. doi: 10.1126/science.aaf2477. PMID:27126043<ref>PMID:27126043</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5doq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Geobacillus sp. pa-3]]
[[Category: Hirose, T]]
[[Category: Kusumoto, T]]
[[Category: Langer, J]]
[[Category: Michel, H]]
[[Category: Mueller, H]]
[[Category: Ovchinnikov, S]]
[[Category: Preu, J]]
[[Category: Rajendran, C]]
[[Category: Safarian, S]]
[[Category: Sakamoto, J]]
[[Category: Bd oxidase]]
[[Category: Oxidoreductase]]
[[Category: Terminal oxidase]]