4e2f

Crystal Structure of E. coli Aspartate Transcarbamoylase K164E/E239K Mutant in an intermediate stateCrystal Structure of E. coli Aspartate Transcarbamoylase K164E/E239K Mutant in an intermediate state

Structural highlights 4e2f is a 12 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Related: 1za1, 1d09 Gene: b4245, JW4204, pyrB (Escherichia coli), b4244, JW4203, pyrI (Escherichia coli) Activity: Aspartate carbamoyltransferase, with EC number 2.1.3.2 Resources: FirstGlance, OCA, RCSB, PDBsum Function [PYRI_ECOLI] Involved in allosteric regulation of aspartate carbamoyltransferase.[HAMAP-Rule:MF_00002] Publication Abstract from PubMed X-ray crystallography and small-angle X-ray scattering (SAXS) in solution have been used to show that a mutant aspartate transcarbamoylase exists in an intermediate quaternary structure between the canonical T and R structures. Additionally, the SAXS data indicate a pH-dependent structural alteration consistent with either a pH-induced conformational change or a pH-induced alteration in the T to R equilibrium. These data indicate that this mutant is not a model for the R state, as has been proposed, but rather represents the enzyme trapped along the path of the allosteric transition between the T and R states. Trapping and structure determination of an intermediate in the allosteric transition of aspartate transcarbamoylase.,Guo W, West JM, Dutton AS, Tsuruta H, Kantrowitz ER Proc Natl Acad Sci U S A. 2012 Apr 30. PMID:22547808 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aspartate carbamoyltransferase

spinqualitylabelsall models 4e2f, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image