Ontology highlight
ABSTRACT:
SUBMITTER: Wang J
PROVIDER: S-EPMC1157055 | biostudies-literature | 2005 Jun
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20050610 25
X-ray structures of aspartate transcarbamoylase in the absence and presence of the first substrate carbamoyl phosphate are reported. These two structures in conjunction with in silico docking experiments provide snapshots of critical events in the function of the enzyme. The ordered substrate binding, observed experimentally, can now be structurally explained by a conformational change induced upon the binding of carbamoyl phosphate. This induced fit dramatically alters the electrostatics of the ...[more]