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| | {{STRUCTURE_1odo| PDB=1odo | SCENE= }} | | {{STRUCTURE_1odo| PDB=1odo | SCENE= }} |
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| - | '''1.85 A STRUCTURE OF CYP154A1 FROM STREPTOMYCES COELICOLOR A3(2)'''
| + | ===1.85 A STRUCTURE OF CYP154A1 FROM STREPTOMYCES COELICOLOR A3(2)=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_14691240}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14691240 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_14691240}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: P450 monooxygenase]] | | [[Category: P450 monooxygenase]] |
| | [[Category: Streptomyce]] | | [[Category: Streptomyce]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:42:47 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:00:56 2008'' |
Revision as of 06:01, 28 July 2008
Template:STRUCTURE 1odo
1.85 A STRUCTURE OF CYP154A1 FROM STREPTOMYCES COELICOLOR A3(2)
Template:ABSTRACT PUBMED 14691240
About this Structure
1ODO is a Single protein structure of sequence from Streptomyces coelicolor. Full crystallographic information is available from OCA.
Reference
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
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