spacer HOLO-(ACYL CARRIER PROTEIN) SYNTHASE IN COMPLEX WITH COENZYME A AT 1.5A
Primary citation
Title Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites.
Authors Parris, K.D.search; Lin, L.search; Tam, A.search; Mathew, R.search; Hixon, J.search; Stahl, M.search; Fritz, C.C.search; Seehra, J.search; Somers, W.S.search
Journal STRUCTUREsearch vol:8, pag:883-895 (2000), Identifiers: PubMed ID (10997907)search DOI (10.1016/S0969-2126(00)00178-7)
Abstract Holo-(acyl carrier protein) synthase (AcpS), a member of the phosphopantetheinyl transferase superfamily, plays a crucial role in the functional activation of acyl carrier protein (ACP) in the fatty acid biosynthesis pathway. AcpS catalyzes the attachment of the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to the sidechain of a conserved serine residue on apo-ACP.
MeSH terms Acyl Carrier Proteinsearch, Amino Acid Sequencesearch, Bacillus subtilissearch, Binding Sitessearch, Molecular Sequence Datasearch, Protein Conformationsearch, Sequence Alignmentsearch, Substrate Specificitysearch, Transferases (Other Substituted Phosphate Groups)search
Other entries described in this publication 1f7t, 1f80
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