Center for Structural Genomics of Infectious Diseases

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Structure of IDP90587

CSGID target: IDP90587
PDB Id: 3LXM (NCBI MMDB)
Authors: 'A.S.Halavaty,G.Minasov,I.Dubrovska,J.Winsor,L.Shuvalova,S.Peterson,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid)'
Responsible person: Andrei Halavaty
Responsible lab: Northwestern University
Deposition Date: Feb 25, 2010
Release Date: Mar 16, 2010

Description: The enzyme aspartate carbamoyltransferase (ATCase) catalyzes the first step in the pyrimidine biosynthetic pathway. Crystal structure of a catalytic (C) subunit of the Yersinia pestis CO92 ATCase was solved by molecular replacement using the structure of the unregulated, N-phosphonacetyl-L-aspartate (PALA)-bound C subunit of ATCase from Escherichia coli (PDB ID 1EKX) as a model. Both proteins share 84 % sequence identity, are trimeric in the crystal and have 1.6 Å root-mean-square deviation (rmsd) of the C-alpha atoms. The structural discrepancy between two proteins is due to the greater overall flexibility and disorder in loops containing active-site residues of the ligand-free Y. pestis C trimer. In contrast, the E.coli PALA-free C trimer (PDB ID 3CSU) has 0.5 Å rmsd of the C-alpha atoms with its Y. pestis homolog. This indicates that binding of a substrate (substrate analog) alters structural perturbations. In order to understand the regulation mechanism of the Y. pestis ATCase, conformational states that account for allosteric structural changes in catalytic activity should be defined.
Functional assignment: Transferase

Ligand code	Name	Ligand type
175	3,5-dihydro-5-methylidene-4h-imidazol-4-on