1za1
Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP at 2.20 A resolution
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OverviewOverview
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, active site, creating a binding pocket for aspartate. Upon aspartate, binding, a further change in electrostatics causes a second induced fit, the domain closure. This domain closure acts as a clamp that both, facilitates catalysis by approximation and also initiates the global, conformational change that manifests homotropic cooperativity.
About this StructureAbout this Structure
1ZA1 is a Protein complex structure of sequences from Escherichia coli with ZN and CTP as ligands. Active as Aspartate carbamoyltransferase, with EC number 2.1.3.2 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase., Wang J, Stieglitz KA, Cardia JP, Kantrowitz ER, Proc Natl Acad Sci U S A. 2005 Jun 21;102(25):8881-6. Epub 2005 Jun 10. PMID:15951418
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