6hif
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Kuenenia stuttgartiensis hydrazine dehydrogenase complex== | |
- | + | <StructureSection load='6hif' size='340' side='right'caption='[[6hif]], [[Resolution|resolution]] 2.80Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[6hif]] is a 36 chain structure with sequence from [http://en.wikipedia.org/wiki/Kuenenia_stuttgartiensis Kuenenia stuttgartiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HIF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HIF FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
- | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrazine_dehydrogenase Hydrazine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.8 1.7.2.8] </span></td></tr> |
- | [[Category: | + | <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=6hif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hif OCA], [http://pdbe.org/6hif PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hif RCSB], [http://www.ebi.ac.uk/pdbsum/6hif PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hif ProSAT]</span></td></tr> |
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/HDH_KUEST HDH_KUEST]] Catalyzes the four-electron oxidation of hydrazine to N2 (PubMed:21964329). The electrons derived from hydrazine oxidation may be transferred to the quinone pool and exploited to promote the generation of proton-motive force (pmf) across the anammoxosome membrane (PubMed:21964329, PubMed:23210799). Is involved in anaerobic ammonium oxidation (anammox), a biological process in which nitrite is used as the electron acceptor in the conversion of ammonium to dinitrogen gas (N2) and water; this bacterial process has a major role in the Earth's nitrogen cycle and has been estimated to synthesize up to 50% of the dinitrogen gas emitted into our atmosphere from the oceans (PubMed:21964329). Cannot oxidize hydroxylamine to NO (PubMed:21964329).<ref>PMID:21964329</ref> <ref>PMID:23210799</ref> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Hydrazine dehydrogenase]] | ||
+ | [[Category: Kuenenia stuttgartiensis]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Akram, M]] | ||
+ | [[Category: Almeida, N M.de]] | ||
+ | [[Category: Barends, T R.M]] | ||
+ | [[Category: Dietl, A]] | ||
[[Category: Ferousi, C]] | [[Category: Ferousi, C]] | ||
- | [[Category: | + | [[Category: Jetten, M S.M]] |
+ | [[Category: Kartal, B]] | ||
+ | [[Category: Keltjens, J]] | ||
[[Category: Maalcke, W]] | [[Category: Maalcke, W]] | ||
- | [[Category: Barends, T.R.M]] | ||
- | [[Category: Jetten, M.S.M]] | ||
- | [[Category: Akram, M]] | ||
- | [[Category: Prinz, S]] | ||
[[Category: Mersdorf, U]] | [[Category: Mersdorf, U]] | ||
- | [[Category: Dietl, A]] | ||
[[Category: Parey, K]] | [[Category: Parey, K]] | ||
- | [[Category: | + | [[Category: Prinz, S]] |
- | [[Category: | + | [[Category: Reimann, J]] |
+ | [[Category: Anammox]] | ||
+ | [[Category: Dehydrogenase]] | ||
+ | [[Category: Hydrazine]] | ||
+ | [[Category: Oxidoreductase]] | ||
+ | [[Category: P460]] | ||
+ | [[Category: Redox]] |
Revision as of 05:57, 17 April 2019
Kuenenia stuttgartiensis hydrazine dehydrogenase complex
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Categories: Hydrazine dehydrogenase | Kuenenia stuttgartiensis | Large Structures | Akram, M | Almeida, N M.de | Barends, T R.M | Dietl, A | Ferousi, C | Jetten, M S.M | Kartal, B | Keltjens, J | Maalcke, W | Mersdorf, U | Parey, K | Prinz, S | Reimann, J | Anammox | Dehydrogenase | Hydrazine | Oxidoreductase | P460 | Redox