4hgh
From Proteopedia
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| - | + | ==Crystal structure of P450 BM3 5F5 heme domain variant complexed with styrene (dataset I)== | |
| - | + | <StructureSection load='4hgh' size='340' side='right' caption='[[4hgh]], [[Resolution|resolution]] 1.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4hgh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HGH FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SYN:ETHENYLBENZENE'>SYN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bu7|1bu7]], [[1jpz|1jpz]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cyp102, cyp102A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 Bacillus megaterium])</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=4hgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hgh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hgh RCSB], [http://www.ebi.ac.uk/pdbsum/4hgh PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Solved crystal structures of P450 BM3 variants in complex with styrene provide on the molecular level a first explanation of how a positively charged surface residue inverts the enantiopreference of styrene epoxidation. The obtained insights into productive and non-productive styrene binding modes deepened our understanding of enantioselective epoxidation with P450 BM3. | ||
| - | + | P450 BM3 crystal structures reveal the role of the charged surface residue Lys/Arg184 in inversion of enantioselective styrene epoxidation.,Shehzad A, Panneerselvam S, Linow M, Bocola M, Roccatano D, Mueller-Dieckmann J, Wilmanns M, Schwaneberg U Chem Commun (Camb). 2013 May 21;49(41):4694-6. doi: 10.1039/c3cc39076d. Epub 2013, Apr 15. PMID:23589805<ref>PMID:23589805</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | [[ | + | </div> |
| + | |||
| + | ==See Also== | ||
| + | *[[Cytochrome P450|Cytochrome P450]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bacillus megaterium]] | [[Category: Bacillus megaterium]] | ||
| - | [[Category: Bocola, M | + | [[Category: Bocola, M]] |
| - | [[Category: Mueller-Dieckmann, J | + | [[Category: Mueller-Dieckmann, J]] |
| - | [[Category: Panneerselvam, S | + | [[Category: Panneerselvam, S]] |
| - | [[Category: Schwaneberg, U | + | [[Category: Schwaneberg, U]] |
| - | [[Category: Shehzad, A | + | [[Category: Shehzad, A]] |
| - | [[Category: Wilmanns, M | + | [[Category: Wilmanns, M]] |
[[Category: Heme binding]] | [[Category: Heme binding]] | ||
[[Category: Hemoprotein]] | [[Category: Hemoprotein]] | ||
Revision as of 13:09, 21 December 2014
Crystal structure of P450 BM3 5F5 heme domain variant complexed with styrene (dataset I)
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