1HY8

SOLUTION STRUCTURE OF B. SUBTILIS ACYL CARRIER PROTEIN

Summary for 1HY8

• Entry DOI: 10.2210/pdb1hy8/pdb
• NMR Information: BMRB: 4989
• Descriptor: ACYL CARRIER PROTEIN (1 entity in total)
• Functional Keywords: apo-acp, holo-acp, acps, fatty acid biosynthesis, 4' phosphopantetheine prosthetic group, lipid binding protein
• Biological source: Bacillus subtilis
• Total number of polymer chains: 1
• Total formula weight: 8466.25

Authors

Xu, G.-Y.,Tam, A.,Lin, L.,Hixon, J.,Fritz, C.C.,Power, R. (deposition date: 2001-01-18, release date: 2002-01-23, Last modification date: 2024-05-22)

Primary citation

Xu, G.Y.,Tam, A.,Lin, L.,Hixon, J.,Fritz, C.C.,Powers, R.
Solution structure of B. subtilis acyl carrier protein.
Structure, 9:277-287, 2001

PubMed Abstract: Acyl carrier protein (ACP) is a fundamental component of fatty acid biosynthesis in which the fatty acid chain is elongated by the fatty acid synthetase system while attached to the 4'-phosphopantetheine prosthetic group (4'-PP) of ACP. Activation of ACP is mediated by holo-acyl carrier protein synthase (ACPS) when ACPS transfers the 4'-PP moiety from coenzyme A (CoA) to Ser36 of apo-ACP. Both ACP and ACPS have been identified as essential for E. coli viability and potential targets for development of antibiotics.

PubMed: 11525165
DOI: 10.1016/S0969-2126(01)00586-X

Experimental method

SOLUTION NMR