2JBZ

Crystal structure of the Streptomyces coelicolor holo-[Acyl-carrier-protein] Synthase (AcpS) in complex with coenzyme A at 1.6 A

Summary for 2JBZ

• Entry DOI: 10.2210/pdb2jbz/pdb
• Related: 2JCA 2WDO 2WDS 2WDY
• Descriptor: HOLO-[ACYL-CARRIER-PROTEIN] SYNTHASE, MAGNESIUM ION, POTASSIUM ION, ... (5 entities in total)
• Functional Keywords: acp, magnesium, coenzyme a, transferase, poliketides, metal- binding, lipid synthesis, phosphopantetheine arm, fatty acid biosynthesis, acyl carrier protein synthase
• Biological source: STREPTOMYCES COELICOLOR
• Cellular location: Cytoplasm (By similarity): O86785
• Total number of polymer chains: 1
• Total formula weight: 15582.71

Authors

Dall'Aglio, P.,Arthur, C.,Law, C.K.E.,Crump, M.P.,Crosby, J.,Hadfield, A.T. (deposition date: 2006-12-15, release date: 2007-01-23, Last modification date: 2024-05-01)

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

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: 21595442
DOI: 10.1021/BI2003668

Experimental method

X-RAY DIFFRACTION (1.62 Å)