Ontology highlight
ABSTRACT:
SUBMITTER: Calisto BM
PROVIDER: S-EPMC2206962 | biostudies-literature | 2007 Sep
REPOSITORIES: biostudies-literature
Calisto Barbara M BM Perez-Gil Jordi J Bergua Maria M Querol-Audi Jordi J Fita Ignacio I Imperial Santiago S
Protein science : a publication of the Protein Society 20070727 9
The X-ray crystal structure of the 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (MCS) from Arabidopsis thaliana has been solved at 2.3 A resolution in complex with a cytidine-5-monophosphate (CMP) molecule. This is the first structure determined of an MCS enzyme from a plant. Major differences between the A. thaliana and bacterial MCS structures are found in the large molecular cavity that forms between subunits and involve residues that are highly conserved among plants. In some bacteri ...[more]