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| | <StructureSection load='6koc' size='340' side='right'caption='[[6koc]], [[Resolution|resolution]] 3.80Å' scene=''> | | <StructureSection load='6koc' size='340' side='right'caption='[[6koc]], [[Resolution|resolution]] 3.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6koc]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835] and [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KOC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KOC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6koc]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] and [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KOC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KOC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=IHQ:2-heptyl-3-iodanyl-1-oxidanyl-quinolin-4-one'>IHQ</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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=IHQ:2-heptyl-3-iodanyl-1-oxidanyl-quinolin-4-one'>IHQ</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6kob|6kob]]</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=6koc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6koc OCA], [https://pdbe.org/6koc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6koc RCSB], [https://www.ebi.ac.uk/pdbsum/6koc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6koc ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">qoxB, B4122_4931, B4417_2140, ETA10_20065, ETK61_21170, ETL41_11350, SC09_contig4orf01211 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835]), qoxA, ETA10_20070, ETK61_21175, ETL41_11355 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835]), B4122_4930, B4417_2139, ETA10_20060, ETK61_21165, ETL41_11345, SC09_contig4orf01209 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835]), qoxD, BSU38140, ipa-40d ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=6koc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6koc OCA], [http://pdbe.org/6koc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6koc RCSB], [http://www.ebi.ac.uk/pdbsum/6koc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6koc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A2I7T8S1_BACIU A0A2I7T8S1_BACIU]] Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I.[PIRNR:PIRNR000292] | + | [https://www.uniprot.org/uniprot/QOX1_BACSU QOX1_BACSU] Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ding, Z]] | + | [[Category: Ding Z]] |
| - | [[Category: Gennis, R B]] | + | [[Category: Gennis RB]] |
| - | [[Category: Li, J]] | + | [[Category: Li J]] |
| - | [[Category: Liu, B]] | + | [[Category: Liu B]] |
| - | [[Category: Xu, J]] | + | [[Category: Xu J]] |
| - | [[Category: Zhu, J]] | + | [[Category: Zhu J]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Inhibitor]]
| + | |
| - | [[Category: Menaquinol oxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Proton pumping]]
| + | |
| Structural highlights
Function
QOX1_BACSU Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth (By similarity).
Publication Abstract from PubMed
Virtually all proton-pumping terminal respiratory oxygen reductases are members of the heme-copper oxidoreductase superfamily. Most of these enzymes use reduced cytochrome c as a source of electrons, but a group of enzymes have evolved to directly oxidize membrane-bound quinols, usually menaquinol or ubiquinol. All of the quinol oxidases have an additional transmembrane helix (TM0) in subunit I that is not present in the related cytochrome c oxidases. The current work reports the 3.6-A-resolution X-ray structure of the cytochrome aa 3 -600 menaquinol oxidase from Bacillus subtilis containing 1 equivalent of menaquinone. The structure shows that TM0 forms part of a cleft to accommodate the menaquinol-7 substrate. Crystals which have been soaked with the quinol-analog inhibitor HQNO (N-oxo-2-heptyl-4-hydroxyquinoline) or 3-iodo-HQNO reveal a single binding site where the inhibitor forms hydrogen bonds to amino acid residues shown previously by spectroscopic methods to interact with the semiquinone state of menaquinone, a catalytic intermediate.
Structure of the cytochrome aa 3 -600 heme-copper menaquinol oxidase bound to inhibitor HQNO shows TM0 is part of the quinol binding site.,Xu J, Ding Z, Liu B, Yi SM, Li J, Zhang Z, Liu Y, Li J, Liu L, Zhou A, Gennis RB, Zhu J Proc Natl Acad Sci U S A. 2020 Jan 14;117(2):872-876. doi:, 10.1073/pnas.1915013117. Epub 2019 Dec 30. PMID:31888984[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu J, Ding Z, Liu B, Yi SM, Li J, Zhang Z, Liu Y, Li J, Liu L, Zhou A, Gennis RB, Zhu J. Structure of the cytochrome aa 3 -600 heme-copper menaquinol oxidase bound to inhibitor HQNO shows TM0 is part of the quinol binding site. Proc Natl Acad Sci U S A. 2020 Jan 14;117(2):872-876. doi:, 10.1073/pnas.1915013117. Epub 2019 Dec 30. PMID:31888984 doi:http://dx.doi.org/10.1073/pnas.1915013117
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