4F04

A Second Allosteric site in E. coli Aspartate Transcarbamoylase: R-state ATCase with UTP bound

Summary for 4F04

Entry DOI	10.2210/pdb4f04/pdb
Descriptor	Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, N-(PHOSPHONACETYL)-L-ASPARTIC ACID, ... (6 entities in total)
Functional Keywords	allosteric regulation, atcase, transferase
Biological source	Escherichia coli More
Total number of polymer chains	4
Total formula weight	104570.80
Authors	Peterson, A.W.,Cockrell, G.M.,Kantrowitz, E.R. (deposition date: 2012-05-03, release date: 2012-07-11, Last modification date: 2024-02-28)
Primary citation	Peterson, A.W.,Cockrell, G.M.,Kantrowitz, E.R. A second allosteric site in Escherichia coli aspartate transcarbamoylase. Biochemistry, 51:4776-4778, 2012 Cited by PubMed Abstract: Escherichia coli aspartate transcarbamoylase is feedback inhibited by CTP and UTP in the presence of CTP. Here, we show by X-ray crystallography that UTP binds to a unique site on each regulatory chain of the enzyme that is near but not overlapping with the known CTP site. These results bring into question all of the previously proposed mechanisms of allosteric regulation in aspartate transcarbamoylase. PubMed: 22667327 DOI: 10.1021/bi3006219 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.3 Å)

Structure validation