2WDY
Crystal structure of the Streptomyces coelicolor D111A AcpS mutant in complex with cofactor CoA at 1.4 A
Summary for 2WDY
| Entry DOI | 10.2210/pdb2wdy/pdb |
| Related | 2JBZ 2JCA 2WDO 2WDS |
| Descriptor | HOLO-[ACYL-CARRIER-PROTEIN] SYNTHASE, MAGNESIUM ION, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | phosphopantetheine arm, fatty acid biosynthesis, lipid synthesis, transferase, polyketides |
| Biological source | STREPTOMYCES COELICOLOR |
| Cellular location | Cytoplasm (By similarity): O86785 |
| Total number of polymer chains | 1 |
| Total formula weight | 15546.90 |
| Authors | Dall'Aglio, P.,Arthur, C.,Crump, M.P.,Crosby, J.,Hadfield, A.T. (deposition date: 2009-03-27, release date: 2010-04-21, Last modification date: 2023-12-13) |
| Primary citation | Dall'Aglio, P.,Arthur, C.,Williams, C.,Vasilakis, K.,Maple, H.J.,Crosby, J.,Crump, M.P.,Hadfield, A.T. Analysis of Streptomyces Coelicolor Phosphopantetheinyl Transferase, Acps, Reveals the Basis for Relaxed Substrate Specificity. Biochemistry, 50:5704-, 2011 Cited by PubMed Abstract: The transfer of the phosphopantetheine chain from coenzyme A (CoA) to the acyl carrier protein (ACP), a key protein in both fatty acid and polyketide synthesis, is catalyzed by ACP synthase (AcpS). Streptomyces coelicolor AcpS is a doubly promiscuous enzyme capable of activation of ACPs from both fatty acid and polyketide synthesis and catalyzes the transfer of modified CoA substrates. Five crystal structures have been determined, including those of ligand-free AcpS, complexes with CoA and acetyl-CoA, and two of the active site mutants, His110Ala and Asp111Ala. All five structures are trimeric and provide further insight into the mechanism of catalysis, revealing the first detailed structure of a group I active site with the essential magnesium in place. Modeling of ACP binding supported by mutational analysis suggests an explanation for the promiscuity in terms of both ACP partner and modified CoA substrates. PubMed: 21595442DOI: 10.1021/BI2003668 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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