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==The structure of bd oxidase from Geobacillus thermodenitrificans== | ==The structure of bd oxidase from Geobacillus thermodenitrificans== | ||
<StructureSection load='5ir6' size='340' side='right' caption='[[5ir6]], [[Resolution|resolution]] 3.80Å' scene=''> | <StructureSection load='5ir6' size='340' side='right'caption='[[5ir6]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ir6]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ir6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_sp._PA-3 Geobacillus sp. PA-3] and [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IR6 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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=5ir6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ir6 OCA], [https://pdbe.org/5ir6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ir6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ir6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ir6 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9Z9N1_GEOSE Q9Z9N1_GEOSE] | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5ir6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome bd oxidase|Cytochrome bd oxidase]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Geobacillus sp. | [[Category: Geobacillus sp. PA-3]] | ||
[[Category: Geobacillus stearothermophilus | [[Category: Geobacillus stearothermophilus]] | ||
[[Category: Hirose | [[Category: Large Structures]] | ||
[[Category: Kusumoto | [[Category: Hirose T]] | ||
[[Category: Langer | [[Category: Kusumoto T]] | ||
[[Category: Michel | [[Category: Langer J]] | ||
[[Category: Mueller | [[Category: Michel H]] | ||
[[Category: Ovchinnikov | [[Category: Mueller H]] | ||
[[Category: Preu | [[Category: Ovchinnikov S]] | ||
[[Category: Rajendran | [[Category: Preu J]] | ||
[[Category: Safarian | [[Category: Rajendran C]] | ||
[[Category: Sakamoto | [[Category: Safarian S]] | ||
[[Category: Sakamoto J]] | |||
Latest revision as of 17:06, 30 August 2023
The structure of bd oxidase from Geobacillus thermodenitrificansThe structure of bd oxidase from Geobacillus thermodenitrificans
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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