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4n4m

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==Kuenenia stuttgartiensis hydroxylamine oxidoreductase soaked in phenyl hydrazine==
==Kuenenia stuttgartiensis hydroxylamine oxidoreductase soaked in phenyl hydrazine==
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<StructureSection load='4n4m' size='340' side='right' caption='[[4n4m]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='4n4m' size='340' side='right'caption='[[4n4m]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4n4m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Candidatus_kuenenia_stuttgartiensis Candidatus kuenenia stuttgartiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N4M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N4M FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4n4m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidatus_Kuenenia_stuttgartiensis Candidatus Kuenenia stuttgartiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N4M FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PHZ:1-PHENYLHYDRAZINE'>PHZ</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n4j|4n4j]], [[4n4k|4n4k]], [[4n4l|4n4l]], [[4n4n|4n4n]], [[4n4o|4n4o]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PHZ:1-PHENYLHYDRAZINE'>PHZ</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydroxylamine_dehydrogenase Hydroxylamine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.6 1.7.2.6] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4n4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4m OCA], [https://pdbe.org/4n4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n4m RCSB], [https://www.ebi.ac.uk/pdbsum/4n4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n4m ProSAT]</span></td></tr>
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<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=4n4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4m OCA], [http://pdbe.org/4n4m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n4m RCSB], [http://www.ebi.ac.uk/pdbsum/4n4m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n4m ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q1PX48_KUEST Q1PX48_KUEST]
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Nitric oxide (NO) is an important molecule in all domains of life with significant biological functions in both pro- and eukaryotes. Anaerobic ammonium-oxidizing (anammox) bacteria that contribute substantially to the release of fixed nitrogen into the atmosphere use the oxidizing power of NO to activate inert ammonium into hydrazine (N2H4). Here, we describe an enzyme from the anammox bacterium Kuenenia stuttgartiensis that uses a novel pathway to make NO from hydroxylamine. This new enzyme is related to octaheme hydroxylamine oxidoreductase (HAO), a key protein in aerobic ammonium-oxidizing bacteria. By a multiphasic approach including the determination of the crystal structure of the K. stuttgartiensis enzyme at 1.8Angstrom resolution and refinement and reassessment of the HAO structure from Nitrosomonas europaea, both in the presence and absence of their substrates, we propose a model for NO formation by the K. stuttgartiensis enzyme. Our results expand the understanding of the functions that the widespread family of octaheme proteins have.
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Structural basis of biological NO generation by octaheme oxidoreductases.,Maalcke WJ, Dietl A, Marritt SJ, Butt JN, Jetten MS, Keltjens JT, Barends TR, Kartal B J Biol Chem. 2013 Dec 3. PMID:24302732<ref>PMID:24302732</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4n4m" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Candidatus kuenenia stuttgartiensis]]
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[[Category: Candidatus Kuenenia stuttgartiensis]]
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[[Category: Hydroxylamine dehydrogenase]]
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[[Category: Large Structures]]
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[[Category: Barends, T R.M B]]
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[[Category: Barends TRMB]]
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[[Category: Butt, J N]]
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[[Category: Butt JN]]
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[[Category: Dietl, A]]
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[[Category: Dietl A]]
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[[Category: Jetten, M S.M]]
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[[Category: Jetten MSM]]
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[[Category: Kartal, B]]
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[[Category: Kartal B]]
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[[Category: Keltjens, J T]]
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[[Category: Keltjens JT]]
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[[Category: Maalcke, W J]]
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[[Category: Maalcke WJ]]
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[[Category: Marritt, S J]]
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[[Category: Marritt SJ]]
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[[Category: C-type cytochrome]]
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[[Category: Oxidoreductase]]
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Current revision

Kuenenia stuttgartiensis hydroxylamine oxidoreductase soaked in phenyl hydrazine

PDB ID 4n4m

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