4n4l
From Proteopedia
(Difference between revisions)
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| - | + | ==Kuenenia stuttgartiensis hydroxylamine oxidoreductase soaked in hydrazine== | |
| - | ===Kuenenia stuttgartiensis hydroxylamine oxidoreductase | + | <StructureSection load='4n4l' size='340' side='right' caption='[[4n4l]], [[Resolution|resolution]] 1.90Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4n4l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"candidatus_kuenenia_stuttgartiensis"_schmid_et_al._2000 "candidatus kuenenia stuttgartiensis" schmid et al. 2000]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N4L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N4L FirstGlance]. <br> | ||
| + | </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=HG1:1-[(4-CYCLOHEXYLBUTANOYL)(2-HYDROXYETHYL)AMINO]-1-DEOXY-D-GLUCITOL'>HG1</scene>, <scene name='pdbligand=HZN:HYDRAZINE'>HZN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n4j|4n4j]], [[4n4k|4n4k]], [[4n4m|4n4m]], [[4n4n|4n4n]], [[4n4o|4n4o]]</td></tr> | ||
| + | <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> | ||
| + | <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=4n4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n4l RCSB], [http://www.ebi.ac.uk/pdbsum/4n4l PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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. | ||
| - | + | 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> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Candidatus kuenenia stuttgartiensis]] | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Candidatus kuenenia stuttgartiensis schmid et al. 2000]] | ||
[[Category: Hydroxylamine dehydrogenase]] | [[Category: Hydroxylamine dehydrogenase]] | ||
| - | [[Category: Barends, T R.M B | + | [[Category: Barends, T R.M B]] |
| - | [[Category: Butt, J N | + | [[Category: Butt, J N]] |
| - | [[Category: Dietl, A | + | [[Category: Dietl, A]] |
| - | [[Category: Jetten, M S.M | + | [[Category: Jetten, M S.M]] |
| - | [[Category: Kartal, B | + | [[Category: Kartal, B]] |
| - | [[Category: Keltjens, J T | + | [[Category: Keltjens, J T]] |
| - | [[Category: Maalcke, W J | + | [[Category: Maalcke, W J]] |
| - | [[Category: Marritt, S J | + | [[Category: Marritt, S J]] |
[[Category: C-type cytochrome]] | [[Category: C-type cytochrome]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 09:51, 20 January 2015
Kuenenia stuttgartiensis hydroxylamine oxidoreductase soaked in hydrazine
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