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1odo

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1.85 A structure of CYP154A1 from Streptomyces coelicolor A3(2)

Structural highlights

1odo is a 1 chain structure with sequence from Streptomyces coelicolor A3(2). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.85Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9KZR7_STRCO

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The genus Streptomyces produces two-thirds of microbially derived antibiotics. Polyketides form the largest and most diverse group of these natural products. Antibiotic diversity of polyketides is generated during their biosynthesis by several means, including postpolyketide modification performed by oxidoreductases, a broad group of enzymes including cytochrome P450 monooxygenases (CYPs). CYPs catalyze site-specific oxidation of macrolide antibiotic precursors significantly affecting antibiotic activity. Efficient manipulation of Streptomyces CYPs in generating new antibiotics will require identification and/or engineering of monooxygenases with activities toward a diverse array of chemical substrates. To begin to link structure to function of CYPs involved in secondary metabolic pathways of industrially important species, we determined the X-ray structure of Streptomyces coelicolor A3(2) CYP154A1 at 1.85 A and analyzed it in the context of the closely related CYP154C1 and more distant CYPs from polyketide synthase (EryF) and nonribosomal peptide synthetase (OxyB) biosynthetic pathways. In contrast to CYP154C1, CYP154A1 reveals an active site inaccessible from the molecular surface, and an absence of catalytic activities observed for CYP154C1. Systematic variations in the amino acid patterns and length of the surface HI loop correlate with degree of rotation of the F and G helices relative to the active site in CYP154A1-related CYPs, presumably regulating the degree of active site accessibility and its dimensions. Heme in CYP154A1 is in a 180 degrees flipped orientation compared with most other structurally determined CYPs.

Comparison of the 1.85 A structure of CYP154A1 from Streptomyces coelicolor A3(2) with the closely related CYP154C1 and CYPs from antibiotic biosynthetic pathways.,Podust LM, Bach H, Kim Y, Lamb DC, Arase M, Sherman DH, Kelly SL, Waterman MR Protein Sci. 2004 Jan;13(1):255-68. PMID:14691240^[1]

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

References

↑ Podust LM, Bach H, Kim Y, Lamb DC, Arase M, Sherman DH, Kelly SL, Waterman MR. Comparison of the 1.85 A structure of CYP154A1 from Streptomyces coelicolor A3(2) with the closely related CYP154C1 and CYPs from antibiotic biosynthetic pathways. Protein Sci. 2004 Jan;13(1):255-68. PMID:14691240

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1odo"

@@ Line 1: / Line 1: @@
 ==1.85 A structure of CYP154A1 from Streptomyces coelicolor A3(2)==
-<StructureSection load='1odo' size='340' side='right' caption='[[1odo]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+<StructureSection load='1odo' size='340' side='right'caption='[[1odo]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1odo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strco Strco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ODO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1odo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ODO 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=PIM:4-PHENYL-1H-IMIDAZOLE'>PIM</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</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=1odo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odo OCA], [http://pdbe.org/1odo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1odo RCSB], [http://www.ebi.ac.uk/pdbsum/1odo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1odo ProSAT]</span></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=PIM:4-PHENYL-1H-IMIDAZOLE'>PIM</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=1odo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odo OCA], [https://pdbe.org/1odo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1odo RCSB], [https://www.ebi.ac.uk/pdbsum/1odo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1odo ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9KZR7_STRCO Q9KZR7_STRCO]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Strco]]
+[[Category: Large Structures]]
-[[Category: Arase, M]]
+[[Category: Arase M]]
-[[Category: Bach, H]]
+[[Category: Bach H]]
-[[Category: Kelly, S L]]
+[[Category: Kelly SL]]
-[[Category: Kim, Y]]
+[[Category: Kim Y]]
-[[Category: Lamb, D C]]
+[[Category: Lamb DC]]
-[[Category: Podust, L M]]
+[[Category: Podust LM]]
-[[Category: Sherman, D H]]
+[[Category: Sherman DH]]
-[[Category: Waterman, M R]]
+[[Category: Waterman MR]]
-[[Category: Cytochrome]]
-[[Category: Oxidoreductase]]
-[[Category: P450 monooxygenase]]
-[[Category: Streptomyce]]

1odo

From Proteopedia

Current revision

1.85 A structure of CYP154A1 from Streptomyces coelicolor A3(2)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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