6a7i: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 6a7i is ~~ON HOLD~~

==CYP154C4 from Streptomyces sp. W2061==

== Structural highlights ==

<table><tr><td colspan='2'>[[6a7i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._JS01 Streptomyces sp. JS01]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A7I 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]] 2.19Å</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=6a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a7i OCA], [https://pdbe.org/6a7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a7i RCSB], [https://www.ebi.ac.uk/pdbsum/6a7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a7i ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/A0A087KD84_9ACTN A0A087KD84_9ACTN]

== 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.

~~Authors:~~ Lee, ~~C.W.~~, Lee, J.H.

Characterization of two steroid hydroxylases from different Streptomyces spp. and their ligand-bound and -unbound crystal structures.,Dangi B, Lee CW, Kim KH, Park SH, Yu EJ, Jeong CS, Park H, Lee JH, Oh TJ FEBS J. 2018 Dec 15. doi: 10.1111/febs.14729. PMID:30552795<ref>PMID:30552795</ref>

~~Description~~: ~~CYP154C4 from Streptomyces sp. W2061~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: Lee~~, J.H~~]]

[[Category: Lee~~, C.W~~]]

==See Also==

*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Streptomyces sp. JS01]]

[[Category: Lee CW]]

[[Category: Lee JH]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6a7i is ON HOLD
+==CYP154C4 from Streptomyces sp. W2061==
+<StructureSection load='6a7i' size='340' side='right'caption='[[6a7i]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6a7i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._JS01 Streptomyces sp. JS01]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A7I 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]] 2.19&#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=6a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a7i OCA], [https://pdbe.org/6a7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a7i RCSB], [https://www.ebi.ac.uk/pdbsum/6a7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a7i ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A087KD84_9ACTN A0A087KD84_9ACTN]
+<div style="background-color:#fffaf0;">
+== 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.
-Authors: Lee, C.W., Lee, J.H.
+Characterization of two steroid hydroxylases from different Streptomyces spp. and their ligand-bound and -unbound crystal structures.,Dangi B, Lee CW, Kim KH, Park SH, Yu EJ, Jeong CS, Park H, Lee JH, Oh TJ FEBS J. 2018 Dec 15. doi: 10.1111/febs.14729. PMID:30552795<ref>PMID:30552795</ref>
-Description: CYP154C4 from Streptomyces sp. W2061
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Lee, J.H]]
+<div class="pdbe-citations 6a7i" style="background-color:#fffaf0;"></div>
-[[Category: Lee, C.W]]
+==See Also==
+*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Streptomyces sp. JS01]]
+[[Category: Lee CW]]
+[[Category: Lee JH]]