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{{STRUCTURE_4hgj|  PDB=4hgj  |  SCENE=  }}
==Crystal structure of P450 BM3 5F5 heme domain variant==
===Crystal structure of P450 BM3 5F5 heme domain variant===
<StructureSection load='4hgj' size='340' side='right' caption='[[4hgj]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
{{ABSTRACT_PUBMED_23589805}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4hgj]] 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=4HGJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HGJ 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></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=4hgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hgj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hgj RCSB], [http://www.ebi.ac.uk/pdbsum/4hgj 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.


==Function==
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>
[[http://www.uniprot.org/uniprot/CPXB_BACME CPXB_BACME]] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450.  


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[4hgj]] 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=4HGJ OCA].
</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 16:02, 21 December 2014

Crystal structure of P450 BM3 5F5 heme domain variantCrystal structure of P450 BM3 5F5 heme domain variant

Structural highlights

4hgj is a 2 chain structure with sequence from Bacillus megaterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:cyp102, cyp102A1 (Bacillus megaterium)
Resources:FirstGlance, OCA, RCSB, PDBsum

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Shehzad A, Panneerselvam S, Linow M, Bocola M, Roccatano D, Mueller-Dieckmann J, Wilmanns M, Schwaneberg U. P450 BM3 crystal structures reveal the role of the charged surface residue Lys/Arg184 in inversion of enantioselective styrene epoxidation. Chem Commun (Camb). 2013 May 21;49(41):4694-6. doi: 10.1039/c3cc39076d. Epub 2013, Apr 15. PMID:23589805 doi:http://dx.doi.org/10.1039/c3cc39076d

4hgj, resolution 1.90Å

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