1K97

Crystal Structure of E. coli Argininosuccinate Synthetase in complex with Aspartate and Citrulline

Summary for 1K97

Entry DOI	10.2210/pdb1k97/pdb
Related	1K92
Descriptor	ARGININOSUCCINATE SYNTHASE, ASPARTIC ACID, CITRULLINE, ... (4 entities in total)
Functional Keywords	n-type atp pyrophosphatase, ligase
Biological source	Escherichia coli
Cellular location	Cytoplasm (Probable): P0A6E4
Total number of polymer chains	1
Total formula weight	51275.55
Authors	Lemke, C.T.,Howell, P.L. (deposition date: 2001-10-26, release date: 2001-12-07, Last modification date: 2023-11-15)
Primary citation	Lemke, C.T.,Howell, P.L. The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis. Structure, 9:1153-1164, 2001 Cited by PubMed Abstract: Argininosuccinate synthetase (AS) is the rate-limiting enzyme of both the urea and arginine-citrulline cycles. In mammals, deficiency of AS leads to citrullinemia, a debilitating and often fatal autosomal recessive urea cycle disorder, whereas its overexpression for sustained nitric oxide production via the arginine-citrulline cycle leads to the potentially fatal hypotension associated with septic and cytokine-induced circulatory shock. PubMed: 11738042 DOI: 10.1016/S0969-2126(01)00683-9 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation