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{{STRUCTURE_4n4k|  PDB=4n4k  |  SCENE=  }}
===Kuenenia stuttgartiensis hydroxylamine oxidoreductase soaked in hydroxylamine===
{{ABSTRACT_PUBMED_24302732}}


==About this Structure==
==Kuenenia stuttgartiensis hydroxylamine oxidoreductase soaked in hydroxylamine==
[[4n4k]] 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=4N4K OCA].  
<StructureSection load='4n4k' size='340' side='right'caption='[[4n4k]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4n4k]] 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=4N4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N4K 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]] 2.2&#8491;</td></tr>
<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=HOA:HYDROXYAMINE'>HOA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4n4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4k OCA], [https://pdbe.org/4n4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n4k RCSB], [https://www.ebi.ac.uk/pdbsum/4n4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n4k ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HAO_KUEST HAO_KUEST] Catalyzes the oxidation of hydroxylamine to nitric oxide with cytochrome c acting as an electron acceptor (PubMed:21964329, PubMed:24302732). Does not oxidize hydroxylamine to nitrite (PubMed:24302732). Also able to catalyze the four-electron oxidation of hydrazine to N(2) in vitro with reduced efficiency; however, this reaction is probably not physiological (PubMed:21964329, PubMed:24302732).<ref>PMID:21964329</ref> <ref>PMID:24302732</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Reference==
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>
<ref group="xtra">PMID:024302732</ref><references group="xtra"/><references/>
 
[[Category: Candidatus kuenenia stuttgartiensis]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Hydroxylamine dehydrogenase]]
</div>
[[Category: Barends, T R.M B.]]
<div class="pdbe-citations 4n4k" style="background-color:#fffaf0;"></div>
[[Category: Butt, J N.]]
== References ==
[[Category: Dietl, A.]]
<references/>
[[Category: Jetten, M S.M.]]
__TOC__
[[Category: Kartal, B.]]
</StructureSection>
[[Category: Keltjens, J T.]]
[[Category: Candidatus Kuenenia stuttgartiensis]]
[[Category: Maalcke, W J.]]
[[Category: Large Structures]]
[[Category: Marritt, S J.]]
[[Category: Barends TRMB]]
[[Category: C-type cytochrome]]
[[Category: Butt JN]]
[[Category: Oxidoreductase]]
[[Category: Dietl A]]
[[Category: Jetten MSM]]
[[Category: Kartal B]]
[[Category: Keltjens JT]]
[[Category: Maalcke WJ]]
[[Category: Marritt SJ]]

Latest revision as of 14:10, 6 November 2024

Kuenenia stuttgartiensis hydroxylamine oxidoreductase soaked in hydroxylamineKuenenia stuttgartiensis hydroxylamine oxidoreductase soaked in hydroxylamine

Structural highlights

4n4k is a 1 chain structure with sequence from Candidatus Kuenenia stuttgartiensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HAO_KUEST Catalyzes the oxidation of hydroxylamine to nitric oxide with cytochrome c acting as an electron acceptor (PubMed:21964329, PubMed:24302732). Does not oxidize hydroxylamine to nitrite (PubMed:24302732). Also able to catalyze the four-electron oxidation of hydrazine to N(2) in vitro with reduced efficiency; however, this reaction is probably not physiological (PubMed:21964329, PubMed:24302732).[1] [2]

Publication Abstract from PubMed

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.

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[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Kartal B, Maalcke WJ, de Almeida NM, Cirpus I, Gloerich J, Geerts W, Op den Camp HJ, Harhangi HR, Janssen-Megens EM, Francoijs KJ, Stunnenberg HG, Keltjens JT, Jetten MS, Strous M. Molecular mechanism of anaerobic ammonium oxidation. Nature. 2011 Oct 2;479(7371):127-30. doi: 10.1038/nature10453. PMID:21964329 doi:http://dx.doi.org/10.1038/nature10453
  2. ↑ Maalcke WJ, Dietl A, Marritt SJ, Butt JN, Jetten MS, Keltjens JT, Barends TR, Kartal B. Structural basis of biological NO generation by octaheme oxidoreductases. J Biol Chem. 2013 Dec 3. PMID:24302732 doi:http://dx.doi.org/10.1074/jbc.M113.525147
  3. ↑ Maalcke WJ, Dietl A, Marritt SJ, Butt JN, Jetten MS, Keltjens JT, Barends TR, Kartal B. Structural basis of biological NO generation by octaheme oxidoreductases. J Biol Chem. 2013 Dec 3. PMID:24302732 doi:http://dx.doi.org/10.1074/jbc.M113.525147

4n4k, resolution 2.20Å

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