6l69: Difference between revisions
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==Crystal structure of CYP154C2 from Streptomyces avermitilis== | |||
<StructureSection load='6l69' size='340' side='right'caption='[[6l69]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L69 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]] 1.5Å</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=6l69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l69 OCA], [https://pdbe.org/6l69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l69 RCSB], [https://www.ebi.ac.uk/pdbsum/6l69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l69 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cytochrome P450 enzymes (P450 or CYP) are some of the most versatile biocatalysts, and offer advantages for oxidizing unreactive C-H bonds in mild conditions. In this study, we identified a novel cytochrome P450 154C2 from Streptomyces avermitilis and characterized its function in 2alpha-hydroxylation of testosterone with regio- and stereoselectivity. To investigate the efficiency of electron transfer, we conducted biotransformation using two different P450 redox partners-RhFRED (RhF reductase domain) from Rhodococcus sp. and Pdx (putidaredoxin)/Pdr (putidaredoxin reductase) from Pseudomonas putida and revealed that RhFRED was more effective than Pdx/Pdr, especially in vivo. The Km and kcat values for testosterone were estimated to be 0.16 +/- 0.05 mM and 0.13 +/- 0.02 min(-1), and kcat/Km was 0.81 min(-1) mM(-1). We also determined the crystal structure of the substrate-free form of CYP154C2 at 1.5 A resolution. The structure has a closed conformation, and the substrate binding pocket is narrow, which can explain the strict substrate specificity of the enzyme. | |||
Regio- and stereoselective hydroxylation of testosterone by a novel cytochrome P450 154C2 from Streptomyces avermitilis.,Wang Q, Ma B, Fushinobu S, Zhang C, Xu LH Biochem Biophys Res Commun. 2020 Feb 5;522(2):355-361. doi:, 10.1016/j.bbrc.2019.11.091. Epub 2019 Nov 22. PMID:31767148<ref>PMID:31767148</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6l69" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome P450 hydroxylase 3D structures|Cytochrome P450 hydroxylase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Fushinobu S]] | |||
[[Category: Xu LH]] | |||
Latest revision as of 13:26, 13 August 2026
Crystal structure of CYP154C2 from Streptomyces avermitilis
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