4f04 | pdb_00004f04

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

spinqualitylabelsall models 4f04, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4f04 is a 4 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PAL, UTP, ZN Gene: b4245, JW4204, pyrB (ECOLI), b4244, JW4203, pyrI (ECOLI) Activity: Aspartate carbamoyltransferase, with EC number 2.1.3.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PYRI_ECOLI] Involved in allosteric regulation of aspartate carbamoyltransferase.[HAMAP-Rule:MF_00002] Publication Abstract from PubMed E. coli aspartate transcarbamoylase is feedback inhibited by CTP and by 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 to 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. A Second Allosteric Site in E. coli Aspartate Transcarbamoylase.,Peterson AW, Cockrell GM, Kantrowitz ER Biochemistry. 2012 Jun 5. PMID:22667327 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aspartate carbamoyltransferase

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