Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 74, Issue 1, Pages 50-60Publisher
WILEY
DOI: 10.1002/prot.22131
Keywords
ACP; type I PKS; natural product; biosynthesis; thioester
Categories
Funding
- NCI NIH HHS [U19 CA113297, R01 CA084374, Y1-CO-1020, CA84374, R01 CA084374-10] Funding Source: Medline
- NHGRI NIH HHS [5T32HG002760, T32 HG002760] Funding Source: Medline
- NIGMS NIH HHS [Y1-GM-1104, T32-GM008505, PSO GM64598] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R01CA084374, U19CA113297] Funding Source: NIH RePORTER
- NATIONAL HUMAN GENOME RESEARCH INSTITUTE [T32HG002760] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM008505, P50GM064598] Funding Source: NIH RePORTER
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Although bacterial iterative Type I polyketide synthases are now known to participate in the biosynthesis of a small set of diverse natural products, the subsequent downstream modification of the resulting polyketide products remains poorly understood. Toward this goal, we report the X-ray structure determination at 2.5 A resolution and preliminary characterization of the putative orsellenic acid P450 oxidase (CalO2) involved in calicheamicin biosynthesis. These studies represent the first crystal structure for a P450 involved in modifying a bacterial iterative Type I polyketide product and suggest the CalO2-catalyzed step may occur after CalO3-catalyzed iodination and may also require a coenzyme A- (CoA) or acyl carrier protein- (ACP) bound substrate. Docking studies also reveal a putative docking site within CalO2 for the CLM orsellinic acid synthase (CalO5) ACP domain which involves a well-ordered helix along the CalO2 active site cavity that is unique compared with other P450 structures.
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