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| | <StructureSection load='6e0x' size='340' side='right'caption='[[6e0x]], [[Resolution|resolution]] 1.97Å' scene=''> | | <StructureSection load='6e0x' size='340' side='right'caption='[[6e0x]], [[Resolution|resolution]] 1.97Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6e0x]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Nitrosomonas_sp._al212 Nitrosomonas sp. al212]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E0X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6e0x]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Nitrosomonas_sp._AL212 Nitrosomonas sp. AL212]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E0X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</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]] 1.974Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NAL212_0896 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=153948 Nitrosomonas sp. AL212])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></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=6e0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e0x OCA], [http://pdbe.org/6e0x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e0x RCSB], [http://www.ebi.ac.uk/pdbsum/6e0x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e0x 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=6e0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e0x OCA], [https://pdbe.org/6e0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e0x RCSB], [https://www.ebi.ac.uk/pdbsum/6e0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e0x ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/F9ZFJ0_9PROT F9ZFJ0_9PROT] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nitrosomonas sp. al212]] | + | [[Category: Nitrosomonas sp. AL212]] |
| - | [[Category: Lancaster, K]] | + | [[Category: Lancaster K]] |
| - | [[Category: Smith, M]] | + | [[Category: Smith M]] |
| - | [[Category: Ammonia-oxidizing bacteria]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Nitrification]]
| + | |
| Structural highlights
Function
F9ZFJ0_9PROT
Publication Abstract from PubMed
Ammonia oxidizing bacteria (AOB) use the cytotoxic, energetic molecule hydroxylamine (NH2OH) as a source of reducing equivalents for cellular respiration. Despite disproportionation or violent decomposition being typical outcomes of reactions of NH2OH with iron, AOB and anammox heme P460 proteins including cytochrome (cyt) P460 and hydroxylamine oxidoreductase (HAO) effect controlled, stepwise oxidation of NH2OH to nitric oxide (NO). Curiously, a recently characterized cyt P460 variant from the AOB Nitrosomonas sp. AL212 is able to form all intermediates of cyt P460 catalysis, but is nevertheless incompetent for NH2OH oxidation. We now show via site-directed mutagenesis, activity assays, spectroscopy, and structural biology that this lack of activity is attributable to the absence of a critical basic glutamate residue in the distal pocket above the heme P460 cofactor. This substitution is the only distinguishing characteristic of a protein that is otherwise effectively structurally and spectroscopically identical to an active variant. This highlights and reinforces a fundamental principal of metalloenzymology: metallocofactor inner-sphere geometric and electronic structures are in many cases insufficient for imbuing reactivity; a precisely defined outer coordination sphere contributed by the polypeptide matrix can be the key differentiator between a metalloenzyme and an unreactive metalloprotein.
Controlling a burn: outer-sphere gating of hydroxylamine oxidation by a distal base in cytochrome P460.,Smith MA, Majer SH, Vilbert AC, Lancaster KM Chem Sci. 2019 Mar 6;10(13):3756-3764. doi: 10.1039/c9sc00195f. eCollection 2019 , Apr 7. PMID:31015919[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Smith MA, Majer SH, Vilbert AC, Lancaster KM. Controlling a burn: outer-sphere gating of hydroxylamine oxidation by a distal base in cytochrome P460. Chem Sci. 2019 Mar 6;10(13):3756-3764. doi: 10.1039/c9sc00195f. eCollection 2019 , Apr 7. PMID:31015919 doi:http://dx.doi.org/10.1039/c9sc00195f
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