View source for 4rm4


==The crystal structure of the versatile cytochrome P450 enzyme CYP109B1 from Bacillus subtilis==
<StructureSection load='4rm4' size='340' side='right'caption='[[4rm4]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rm4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis Bacillus subtilis subsp. subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RM4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RM4 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></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU12210, genomic DNA, yjiB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=135461 Bacillus subtilis subsp. subtilis])</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=4rm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rm4 OCA], [http://pdbe.org/4rm4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rm4 RCSB], [http://www.ebi.ac.uk/pdbsum/4rm4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rm4 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the versatile CYP109B1 enzyme from Bacillus subtilis has been solved at 1.8 A resolution. This is the first structure of an enzyme from this CYP family, whose members are prevalent across diverse species of bacteria. In the crystal structure the enzyme has an open conformation with an access channel leading from the heme to the surface. The substrate-free structure reveals the location of the key residues in the active site that are responsible for binding the substrate in the correct orientation for regioselective oxidation. Importantly, there are significant differences among these residues in members of the CYP109 and closely related CYP106 families and these likely account for the variations in substrate binding and oxidation profiles observed with these enzymes. A whole-cell oxidation biosystem was developed, which contains CYP109B1 and a phthalate family oxygenase reductase (PFOR), from Pseudomonas putida KT24440, as the electron transfer partner. This electron transfer system is able to support CYP109B1 activity resulting in the regioselective hydroxylation of both alpha- and beta-ionone in vivo and in vitro. The PFOR is therefore a versatile electron transfer partner that is able to support the activity of CYP enzymes from other bacterium. The crystal structure of CYP109B1 has a positively charged proximal face and this explains why it can interact with PFOR and adrenodoxin which are predominantly negatively charged around their [2Fe-2S] clusters.

The crystal structure of the versatile cytochrome P450 enzyme CYP109B1 from Bacillus subtilis.,Zhang A, Zhang T, Hall EA, Hutchinson S, Cryle MJ, Wong LL, Zhou W, Bell SG Mol Biosyst. 2015 Jan 14. PMID:25587700<ref>PMID:25587700</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4rm4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cytochrome P450|Cytochrome P450]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis subsp. subtilis]]
[[Category: Large Structures]]
[[Category: Bell, S G]]
[[Category: Cryle, M J]]
[[Category: Hall, E A]]
[[Category: Hutchinson, S]]
[[Category: Wong, L L]]
[[Category: Zhang, A L]]
[[Category: Zhang, T]]
[[Category: Zhouw, W H]]
[[Category: Catabolism]]
[[Category: Cytochrome p450]]
[[Category: Electron transport]]
[[Category: Secondary metabolites biosynthesis]]
[[Category: Transport]]