5bv5: Difference between revisions
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==Structure of CYP119 with T213A and C317H mutations== | ==Structure of CYP119 with T213A and C317H mutations== | ||
<StructureSection load='5bv5' size='340' side='right' caption='[[5bv5]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='5bv5' size='340' side='right' caption='[[5bv5]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5bv5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BV5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BV5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5bv5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BV5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BV5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PIM:4-PHENYL-1H-IMIDAZOLE'>PIM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PIM:4-PHENYL-1H-IMIDAZOLE'>PIM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5bv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bv5 OCA], [http://pdbe.org/5bv5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bv5 RCSB], [http://www.ebi.ac.uk/pdbsum/5bv5 PDBsum]</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=5bv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bv5 OCA], [http://pdbe.org/5bv5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bv5 RCSB], [http://www.ebi.ac.uk/pdbsum/5bv5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bv5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 35091]] | |||
[[Category: Arnold, F H]] | [[Category: Arnold, F H]] | ||
[[Category: Buller, A R]] | [[Category: Buller, A R]] | ||
Revision as of 15:23, 6 November 2017
Structure of CYP119 with T213A and C317H mutationsStructure of CYP119 with T213A and C317H mutations
Structural highlights
Publication Abstract from PubMedAlmost all known members of the cytochrome P450 (CYP) superfamily conserve a key cysteine residue that coordinates the heme iron. Although mutation of this residue abolishes monooxygenase activity, recent work has shown that mutation to either serine or histidine unlocks non-natural carbene- and nitrene-transfer activities. Here we present the first crystal structure of a histidine-ligated P450. The T213A/C317H variant of the thermostable CYP119 from Sulfolobus acidocaldarius maintains heme iron coordination through the introduced ligand, an interaction that is accompanied by large changes in the overall protein structure. We also find that the axial cysteine C317 may be substituted with any other amino acid without abrogating folding and heme cofactor incorporation. Several of the axial mutants display unusual spectral features, suggesting that they have active sites with unique steric and electronic properties. These novel, highly stable enzyme active sites will be fruitful starting points for investigations of non-natural P450 catalysis and mechanisms. Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450.,McIntosh JA, Heel T, Buller AR, Chio L, Arnold FH J Am Chem Soc. 2015 Nov 4;137(43):13861-5. doi: 10.1021/jacs.5b07107. Epub 2015, Sep 23. PMID:26299431[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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