6a7j

<StructureSection load='6a7j' size='340' side='right' caption='[[6a7j]], [[Resolution|resolution]] 2.71&Aring;' scene=''>

<table><tr><td colspan='2'>[[6a7j]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A7J 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>, <scene name='pdbligand=TES:TESTOSTERONE'>TES</scene></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=6a7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a7j OCA], [http://pdbe.org/6a7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a7j RCSB], [http://www.ebi.ac.uk/pdbsum/6a7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a7j ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Bacterial cytochrome P450 (CYP) enzymes are involved in the hydroxylation of various endogenous substrates while using a heme molecule as a cofactor. CYPs have gained biotechnological interest as useful biocatalysts capable of altering chemical structures by adding a hydroxyl group in a regiospecific manner. Here, we identified, purified, and characterized two CYP154C4 proteins from Streptomyces sp. W2061 (StCYP154C4-1) and Streptomyces sp. ATCC 11861 (StCYP154C4-2). Activity assays showed that both StCYP154C4-1 and StCYP154C4-2 can produce 2'-hydroxylated testosterone, which differs from the activity of a previously described NfCYP154C5 from Nocardia farcinica in terms of its 16alpha-hydroxylation of testosterone. To better understand the molecular basis of the regioselectivity of these two CYP154C4 proteins, crystal structures of the ligand-unbound form of StCYP154C4-1 and the testosterone-bound form of StCYP154C4-2 were determined. Comparison with the previously determined NfCYP154C5 structure revealed differences in the substrate-binding residues, suggesting a likely explanation for the different patterns of testosterone hydroxylation, despite the high sequence similarities between the enzymes (54% identity). These findings provide valuable insights that will enable protein engineering for the development of artificial steroid-related CYPs exhibiting different regiospecificity.

 

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== References ==

[[Category: Lee, C W]]

[[Category: Lee, J H]]

[[Category: Cytochrome p450]]

[[Category: Oxidoreductase]]

[[Category: Streptomyce]]