|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='2wiy' size='340' side='right'caption='[[2wiy]], [[Resolution|resolution]] 1.49Å' scene=''> | | <StructureSection load='2wiy' size='340' side='right'caption='[[2wiy]], [[Resolution|resolution]] 1.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wiy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"prescottella"_jones_et_al._2013 "prescottella" jones et al. 2013]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WIY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WIY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wiy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus Rhodococcus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WIY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WIY 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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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]] 1.49Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wiv|2wiv]]</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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2wiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wiy OCA], [http://pdbe.org/2wiy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wiy RCSB], [http://www.ebi.ac.uk/pdbsum/2wiy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wiy 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=2wiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wiy OCA], [https://pdbe.org/2wiy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wiy RCSB], [https://www.ebi.ac.uk/pdbsum/2wiy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wiy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8GPH7_RHORH Q8GPH7_RHORH] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 31: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Prescottella jones et al. 2013]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bruce, N C]] | + | [[Category: Rhodococcus]] |
| - | [[Category: Grogan, G]] | + | [[Category: Bruce NC]] |
| - | [[Category: Jackson, R]] | + | [[Category: Grogan G]] |
| - | [[Category: Sabbadin, F]] | + | [[Category: Jackson R]] |
| - | [[Category: Bioremediation]]
| + | [[Category: Sabbadin F]] |
| - | [[Category: Cyt-p450]]
| + | |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Rdx]]
| + | |
| Structural highlights
Function
Q8GPH7_RHORH
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
XplA is a cytochrome P450 of unique structural organization, consisting of a heme-domain that is C-terminally fused to its native flavodoxin redox partner. XplA, along with flavodoxin reductase XplB, has been shown to catalyze the breakdown of the nitramine explosive and pollutant hexahydro-1,3,5-trinitro-1,3,5-triazine (royal demolition explosive) by reductive denitration. The structure of the heme domain of XplA (XplA-heme) has been solved in two crystal forms: as a dimer in space group P2(1) to a resolution of 1.9 A and as a monomer in space group P2(1)2(1)2 to a resolution of 1.5 A, with the ligand imidazole bound at the heme iron. Although it shares the overall fold of cytochromes P450 of known structure, XplA-heme is unusual in that the kinked I-helix that traverses the distal face of the heme is broken by Met-394 and Ala-395 in place of the well conserved Asp/Glu plus Thr/Ser, important in oxidative P450s for the scission of the dioxygen bond prior to substrate oxygenation. The heme environment of XplA-heme is hydrophobic, featuring a cluster of three methionines above the heme, including Met-394. Imidazole was observed bound to the heme iron and is in close proximity to the side chain of Gln-438, which is situated over the distal face of the heme. Imidazole is also hydrogen-bonded to a water molecule that sits in place of the threonine side-chain hydroxyl exemplified by Thr-252 in Cyt-P450cam. Both Gln-438 --> Ala and Ala-395 --> Thr mutants of XplA-heme displayed markedly reduced activity compared with the wild type for royal demolition explosive degradation when combined with surrogate electron donors.
The 1.5-A structure of XplA-heme, an unusual cytochrome P450 heme domain that catalyzes reductive biotransformation of royal demolition explosive.,Sabbadin F, Jackson R, Haider K, Tampi G, Turkenburg JP, Hart S, Bruce NC, Grogan G J Biol Chem. 2009 Oct 9;284(41):28467-75. Epub 2009 Aug 19. PMID:19692330[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sabbadin F, Jackson R, Haider K, Tampi G, Turkenburg JP, Hart S, Bruce NC, Grogan G. The 1.5-A structure of XplA-heme, an unusual cytochrome P450 heme domain that catalyzes reductive biotransformation of royal demolition explosive. J Biol Chem. 2009 Oct 9;284(41):28467-75. Epub 2009 Aug 19. PMID:19692330 doi:10.1074/jbc.M109.031559
|
