Ontology highlight
ABSTRACT:
SUBMITTER: Jung JW
PROVIDER: S-EPMC2144687 | biostudies-other | 2000 Jul
REPOSITORIES: biostudies-other
Jung J W JW An J H JH Na K B KB Kim Y S YS Lee W W
Protein science : a publication of the Protein Society 20000701 7
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 sever ...[more]