View source for 8hg9


==Cytochrome P450 steroid hydroxylase (BaCYP106A6) from Bacillus species==
<StructureSection load='8hg9' size='340' side='right'caption='[[8hg9]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8hg9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._(in:_Bacteria) Bacillus sp. (in: Bacteria)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HG9 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]] 2.79&#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></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=8hg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hg9 OCA], [https://pdbe.org/8hg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hg9 RCSB], [https://www.ebi.ac.uk/pdbsum/8hg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hg9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E5WPM6_9BACI E5WPM6_9BACI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytochrome P450 (CYP) is a heme-containing enzyme that catalyzes hydroxylation reactions with various substrate molecules. Steroid hydroxylases are particularly useful for effectively introducing hydroxyl groups into a wide range of steroids in the pharmaceutical industry. This study reports a newly identified CYP steroid hydroxylase (BaCYP106A6) from the bacterium Bacillus sp. and characterizes it using an in vitro enzyme assay and structural investigation. Bioconversion assays indicated that BaCYP106A1 catalyzes the hydroxylation of progesterone and androstenedione, whereas no or low conversion was observed with 11beta-hydroxysteroids such as cortisol, corticosterone, dexamethasone, and prednisolone. In addition, the crystal structure of BaCYP106A6 was determined at a resolution of 2.8 A to investigate the configuration of the substrate-binding site and understand substrate preference. This structural characterization and comparison with other bacterial steroid hydroxylase CYPs allowed us to identify a unique Arg295 residue that may serve as the key residue for substrate specificity and regioselectivity in BaCYP106A6. This observation provides valuable background for further protein engineering to design commercially useful CYP steroid hydroxylases with different substrate specificities.

Crystal Structure and Biochemical Analysis of a Cytochrome P450 Steroid Hydroxylase (BaCYP106A6) from Bacillus Species.,Kim KH, Do H, Lee CW, Subedi P, Choi M, Nam Y, Lee JH, Oh TJ J Microbiol Biotechnol. 2023 Mar 28;33(3):387-397. doi: 10.4014/jmb.2211.11031. , Epub 2022 Dec 12. PMID:36655276<ref>PMID:36655276</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8hg9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Do H]]
[[Category: Lee JH]]