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Protein Science, Vol 9, Issue 7 1294-1303, Copyright © 2000 by The Protein Society

The active site and substrates binding mode of malonyl-CoA synthetase determined by transferred nuclear Overhauser effect spectroscopy, site- directed mutagenesis, and comparative modeling studies [In Process Citation]

JW Jung, JH An, KB Na, YS Kim and W Lee
Department of Biochemistry, College of Science, Yonsei University, Shinchon-Dong, Seoul, Korea.

The active sites and substrate bindings of Rhizobium trifolii molonyl- CoA synthetase (MCS) catalyzing the malonyl-CoA formation from malonate and CoA have been determined based on NMR spectroscopy, site-directed mutagenesis, and comparative modeling methods. The MCS-bound conformation of malonyl-CoA was determined from two-dimensional- transferred nuclear Overhauser effect spectroscopy data. MCS protein folds into two structural domains and consists of 16 alpha-helices, 24 beta-strands, and several long loops. The core active site was determined as a wide cleft close to the end of the small C-terminal domain. The catalytic substrate malonate is placed between ATP and His206 in the MCS enzyme, supporting His206 in its catalytic role as it generates reaction intermediate, malonyl-AMP. These findings are strongly supported by previous biochemical data, as well as by the site- directed mutagenesis data reported here. This structure reveals the biochemical role as well as the substrate specificity that conservative residues of adenylate-forming enzymes have.
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L. Zhang, A. K. Joshi, and S. Smith
Cloning, Expression, Characterization, and Interaction of Two Components of a Human Mitochondrial Fatty Acid Synthase: MALONYLTRANSFERASE AND ACYL CARRIER PROTEIN
J. Biol. Chem., October 10, 2003; 278(41): 40067 - 40074.
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