4fas
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fas]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Nitrosomonas_europaea_ATCC_19718 Nitrosomonas europaea ATCC 19718]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FAS FirstGlance]. <br> | <table><tr><td colspan='2'>[[4fas]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Nitrosomonas_europaea_ATCC_19718 Nitrosomonas europaea ATCC 19718]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FAS FirstGlance]. <br> | ||
| - | </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=ISW:{3,3-[(9S)-8,13-DIETHENYL-3,7,12,17-TETRAMETHYL-9,10-DIHYDROPORPHYRIN-2,18-DIYL-KAPPA~4~N~21~,N~22~,N~23~,N~24~]DIPROPANOATO(2-)}IRON'>ISW</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=ISW:{3,3-[(9S)-8,13-DIETHENYL-3,7,12,17-TETRAMETHYL-9,10-DIHYDROPORPHYRIN-2,18-DIYL-KAPPA~4~N~21~,N~22~,N~23~,N~24~]DIPROPANOATO(2-)}IRON'>ISW</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=4fas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fas OCA], [https://pdbe.org/4fas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fas RCSB], [https://www.ebi.ac.uk/pdbsum/4fas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fas ProSAT]</span></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=4fas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fas OCA], [https://pdbe.org/4fas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fas RCSB], [https://www.ebi.ac.uk/pdbsum/4fas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fas ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/HAO_NITEU HAO_NITEU] | [https://www.uniprot.org/uniprot/HAO_NITEU HAO_NITEU] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Hydroxylamine oxidoreductase (HAO) is a 24-heme homotrimeric enzyme that catalyzes the conversion of hydroxylamine to nitrite in nitrifying bacteria: a key reaction in the nitrogen cycle. One heme in each HAO monomer is a highly unusual heme P460 that is the site of catalysis. This was proposed to be a c-type heme that contained an additional porphyrin-tyrosine cross-link. Here, we report the crystal structure of HAO from Nitrosomonas europaea to 2.1 A resolution that defines a different model compatible with the crystallographic and biochemical data. The structure reveals that heme P460 contains two covalent cross-links between the porphyrin and a Tyr residue. In addition, the enzyme was purified from source, and an unknown physiological HAO binding partner was present within the crystal (annotated in the genome as hypothetical protein NE1300). NE1300 may play a structural role in the ternary complex with cytochrome c554, the physiological electron acceptor of HAO. | ||
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| - | Structural Studies of Hydroxylamine Oxidoreductase Reveal a Unique Heme Cofactor and a Previously Unidentified Interaction Partner.,Cedervall P, Hooper AB, Wilmot CM Biochemistry. 2013 Aug 26. PMID:23952581<ref>PMID:23952581</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4fas" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 15:20, 14 March 2024
Complex crystal structure of hydroxylamine oxidoreductase and NE1300 from Nitrosomonas europaea
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