1F7L

HOLO-(ACYL CARRIER PROTEIN) SYNTHASE IN COMPLEX WITH COENZYME A AT 1.5A

Summary for 1F7L

• Entry DOI: 10.2210/pdb1f7l/pdb
• Descriptor: HOLO-(ACYL CARRIER PROTEIN) SYNTHASE, CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: 9-strand pseudo beta barrel protein, coa complex protein, coenzyme a complex, transferase
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm : P96618
• Total number of polymer chains: 1
• Total formula weight: 14517.77

Authors

Parris, K.D.,Lin, L.,Tam, A.,Mathew, R.,Hixon, J.,Stahl, M.,Fritz, C.C.,Seehra, J.,Somers, W.S. (deposition date: 2000-06-27, release date: 2001-06-27, Last modification date: 2023-08-09)

Primary citation

Parris, K.D.,Lin, L.,Tam, A.,Mathew, R.,Hixon, J.,Stahl, M.,Fritz, C.C.,Seehra, J.,Somers, W.S.
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.
Structure Fold.Des., 8:883-895, 2000

PubMed 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.

PubMed: 10997907
DOI: 10.1016/S0969-2126(00)00178-7

Experimental method

X-RAY DIFFRACTION (1.5 Å)