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==Crystal structure of the CYP102A5 haem Domain isolated from Bacillus cereus==
<StructureSection load='8hkj' size='340' side='right'caption='[[8hkj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8hkj]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HKJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></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=8hkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hkj OCA], [https://pdbe.org/8hkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hkj RCSB], [https://www.ebi.ac.uk/pdbsum/8hkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hkj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C102_BACCR C102_BACCR] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions, yielding primarily omega-1 and omega-2 hydroxylated products. Metabolizes unsaturated and saturated fatty acids as well as N-acylamino acids. Has a preference for long-chain unsaturated fatty acids over saturated fatty acids. Shows activity toward saturated fatty acids with a chain length of 9-18 carbons with preference for longer fatty acids. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain.<ref>PMID:17945181</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytochrome P450 enzymes (CYPs) have attracted much promise as biocatalysts in a push for cleaner and more environmentally friendly catalytic systems. However, changing the substrate specificity of CYPs, such as CYP102A1, can be a challenging task, requiring laborious mutagenesis. An alternative approach is the use of decoy molecules that "trick" the enzyme into becoming active by impersonating the native substrate. Whilst the decoy molecule system has been extensively developed for CYP102A1, its general applicability for other CYP102-family enzymes has yet to be shown. Herein, we demonstrate that decoy molecules can "trick" CYP102A5 and A7 into becoming active and hydroxylating non-native substrates. Furthermore, significant differences in decoy molecule selectivity as well as decoy molecule binding were observed. The X-ray crystal structure of the CYP102A5 haem domain was solved at 2.8 A, delivering insight into a potential substate-binding site that differs significantly from CYP102A1.

Investigating the applicability of the CYP102A1-decoy-molecule system to other members of the CYP102A subfamily.,Stanfield JK, Onoda H, Ariyasu S, Kasai C, Burfoot EM, Sugimoto H, Shoji O J Inorg Biochem. 2023 Aug;245:112235. doi: 10.1016/j.jinorgbio.2023.112235. Epub , 2023 Apr 20. PMID:37167731<ref>PMID:37167731</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8hkj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus cereus]]
[[Category: Large Structures]]
[[Category: Onoda H]]
[[Category: Shoji O]]
[[Category: Stanfield JK]]
[[Category: Sugimoto H]]