View source for 3ayg


==Crystal structure of nitric oxide reductase complex with HQNO==
<StructureSection load='3ayg' size='340' side='right'caption='[[3ayg]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ayg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AYG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AYG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HQO:2-HEPTYL-4-HYDROXY+QUINOLINE+N-OXIDE'>HQO</scene>, <scene name='pdbligand=LOP:(1R)-2-{[(R)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(DODECANOYLOXY)METHYL]ETHYL+(9Z)-OCTADEC-9-ENOATE'>LOP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3ayg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ayg OCA], [https://pdbe.org/3ayg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ayg RCSB], [https://www.ebi.ac.uk/pdbsum/3ayg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ayg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B3Y963_GEOSE B3Y963_GEOSE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of quinol-dependent nitric oxide reductase (qNOR) from G. stearothermophilus, which catalyzes the reduction of NO to produce the major ozone-depleting gas N(2)O, has been characterized at 2.5 A resolution. The overall fold of qNOR is similar to that of cytochrome c-dependent NOR (cNOR), and some structural features that are characteristic of cNOR, such as the calcium binding site and hydrophilic cytochrome c domain, are observed in qNOR, even though it harbors no heme c. In contrast to cNOR, structure-based mutagenesis and molecular dynamics simulation studies of qNOR suggest that a water channel from the cytoplasm can serve as a proton transfer pathway for the catalytic reaction. Further structural comparison of qNOR with cNOR and aerobic and microaerobic respiratory oxidases elucidates their evolutionary relationship and possible functional conversions.

Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus.,Matsumoto Y, Tosha T, Pisliakov AV, Hino T, Sugimoto H, Nagano S, Sugita Y, Shiro Y Nat Struct Mol Biol. 2012 Jan 22;19(2):238-45. doi: 10.1038/nsmb.2213. PMID:22266822<ref>PMID:22266822</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ayg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Large Structures]]
[[Category: Hino T]]
[[Category: Matsumoto Y]]
[[Category: Nagano S]]
[[Category: Pisliakov AV]]
[[Category: Shiro Y]]
[[Category: Sugimoti H]]
[[Category: Sugita Y]]
[[Category: Tosha T]]