3tzo: Difference between revisions

Latest revision as of 10:21, 13 August 2026

The role of I87 of CYP158A2 in oxidative coupling reaction

Structural highlights

3tzo is a 2 chain structure with sequence from Streptomyces coelicolor. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.76Å
Ligands:	HEM, SPM
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

C1582_STRCO Catalyze oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments which protect the soil bacterium from deleterious effects of UV irradiation (three isomers of biflaviolin and one triflaviolin).^[1] ^[2]

Publication Abstract from PubMed

Both CYP158A1 and CYP158A2 are able to catalyze an oxidative C-C coupling reaction producing biflaviolin or triflaviolin in Streptomyces coelicolor A3(2). The substrate-bound crystal structures of CYP158A2 and CYP158A1 reveal that the side chain of Ile87 in CYP158A2 points to the active site contacting the distal flaviolin molecule, however, the bulkier side chain of Lys90 in CYP158A1 (corresponding to Ile87 in CYP158A2) is toward the distal surface of the protein. These results suggest that these residues could be important in determining product regiospecificity. In order to explore the role of the two residues in catalysis, the reciprocal mutants, Ile87Lys and Lys90Ile, of CYP158A2 and CYP158A1, respectively, were generated and characterized. The mutant Ile87Lys enzyme forms two isomers of biflaviolin instead of three isomers of biflaviolin in wild-type CYP158A2. CYP158A1 containing the substitution of lysine with isoleucine has the same catalytic activity compared with the wild-type CYP158A1. The crystal structure of Ile87Lys showed that the BC loop in the mutant is in a very different orientation compared with the BC loop in both CYP158A1/A2 structures. These results shed light on the mechanism of the oxidative coupling reaction catalyzed by cytochrome P450.

The role of Ile87 of CYP158A2 in oxidative coupling reaction.,Zhao B, Bellamine A, Lei L, Waterman MR Arch Biochem Biophys. 2011 Dec 19. PMID:22203090^[3]

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

References

↑ Zhao B, Guengerich FP, Bellamine A, Lamb DC, Izumikawa M, Lei L, Podust LM, Sundaramoorthy M, Kalaitzis JA, Reddy LM, Kelly SL, Moore BS, Stec D, Voehler M, Falck JR, Shimada T, Waterman MR. Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2. J Biol Chem. 2005 Mar 25;280(12):11599-607. Epub 2005 Jan 19. PMID:15659395 doi:https://dx.doi.org/10.1074/jbc.M410933200
↑ Zhao B, Guengerich FP, Voehler M, Waterman MR. Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer. J Biol Chem. 2005 Dec 23;280(51):42188-97. Epub 2005 Oct 20. PMID:16239228 doi:10.1074/jbc.M509220200
↑ Zhao B, Bellamine A, Lei L, Waterman MR. The role of Ile87 of CYP158A2 in oxidative coupling reaction. Arch Biochem Biophys. 2011 Dec 19. PMID:22203090 doi:10.1016/j.abb.2011.12.007

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Zhao B, Guengerich FP, Bellamine A, Lamb DC, Izumikawa M, Lei L, Podust LM, Sundaramoorthy M, Kalaitzis JA, Reddy LM, Kelly SL, Moore BS, Stec D, Voehler M, Falck JR, Shimada T, Waterman MR. Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2. J Biol Chem. 2005 Mar 25;280(12):11599-607. Epub 2005 Jan 19. PMID:15659395 doi:https://dx.doi.org/10.1074/jbc.M410933200

[2] Zhao B, Guengerich FP, Voehler M, Waterman MR. Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer. J Biol Chem. 2005 Dec 23;280(51):42188-97. Epub 2005 Oct 20. PMID:16239228 doi:10.1074/jbc.M509220200

[3] Zhao B, Bellamine A, Lei L, Waterman MR. The role of Ile87 of CYP158A2 in oxidative coupling reaction. Arch Biochem Biophys. 2011 Dec 19. PMID:22203090 doi:10.1016/j.abb.2011.12.007

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-[[Image:3tzo.png|left|200px]]
-<!--
+==The role of I87 of CYP158A2 in oxidative coupling reaction==
-The line below this paragraph, containing "STRUCTURE_3tzo", creates the "Structure Box" on the page.
+<StructureSection load='3tzo' size='340' side='right'caption='[[3tzo]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3tzo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TZO FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#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=SPM:SPERMINE'>SPM</scene></td></tr>
-{{STRUCTURE_3tzo|  PDB=3tzo  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tzo OCA], [https://pdbe.org/3tzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tzo RCSB], [https://www.ebi.ac.uk/pdbsum/3tzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tzo ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/C1582_STRCO C1582_STRCO] Catalyze oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments which protect the soil bacterium from deleterious effects of UV irradiation (three isomers of biflaviolin and one triflaviolin).<ref>PMID:15659395</ref> <ref>PMID:16239228</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Both CYP158A1 and CYP158A2 are able to catalyze an oxidative C-C coupling reaction producing biflaviolin or triflaviolin in Streptomyces coelicolor A3(2). The substrate-bound crystal structures of CYP158A2 and CYP158A1 reveal that the side chain of Ile87 in CYP158A2 points to the active site contacting the distal flaviolin molecule, however, the bulkier side chain of Lys90 in CYP158A1 (corresponding to Ile87 in CYP158A2) is toward the distal surface of the protein. These results suggest that these residues could be important in determining product regiospecificity. In order to explore the role of the two residues in catalysis, the reciprocal mutants, Ile87Lys and Lys90Ile, of CYP158A2 and CYP158A1, respectively, were generated and characterized. The mutant Ile87Lys enzyme forms two isomers of biflaviolin instead of three isomers of biflaviolin in wild-type CYP158A2. CYP158A1 containing the substitution of lysine with isoleucine has the same catalytic activity compared with the wild-type CYP158A1. The crystal structure of Ile87Lys showed that the BC loop in the mutant is in a very different orientation compared with the BC loop in both CYP158A1/A2 structures. These results shed light on the mechanism of the oxidative coupling reaction catalyzed by cytochrome P450.
-===The role of I87 of CYP158A2 in oxidative coupling reaction===
+The role of Ile87 of CYP158A2 in oxidative coupling reaction.,Zhao B, Bellamine A, Lei L, Waterman MR Arch Biochem Biophys. 2011 Dec 19. PMID:22203090<ref>PMID:22203090</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_22203090}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3tzo" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 22203090 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_22203090}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[3tzo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TZO OCA].
-==Reference==
-<ref group="xtra">PMID:022203090</ref><references group="xtra"/>
 [[Category: Streptomyces coelicolor]]
-[[Category: Waterman, M R.]]
+[[Category: Waterman MR]]
-[[Category: Zhao, B.]]
+[[Category: Zhao B]]
-[[Category: Cyp158a2]]
-[[Category: Monooxygenase]]
-[[Category: Oxidoreductase]]
-[[Category: P450]]
-[[Category: Phenolic coupling reaction]]

3tzo: Difference between revisions

Latest revision as of 10:21, 13 August 2026

The role of I87 of CYP158A2 in oxidative coupling reaction

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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