3ql0 | pdb_00003ql0

Crystal structure of N23PP/S148A mutant of E. coli dihydrofolate reductase

spinqualitylabelsall models 3ql0, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ql0 is a 1 chain structure with sequence from Ecout. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FOL, NA, NAP Related: 3ql3 Gene: folA, UTI89_C0054 (ECOUT) Activity: Dihydrofolate reductase, with EC number 1.5.1.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Conformational dynamics play a key role in enzyme catalysis. Although protein motions have clear implications for ligand flux, a role for dynamics in the chemical step of enzyme catalysis has not been clearly established. We generated a mutant of Escherichia coli dihydrofolate reductase that abrogates millisecond-time-scale fluctuations in the enzyme active site without perturbing its structural and electrostatic preorganization. This dynamic knockout severely impairs hydride transfer. Thus, we have found a link between conformational fluctuations on the millisecond time scale and the chemical step of an enzymatic reaction, with broad implications for our understanding of enzyme mechanisms and for design of novel protein catalysts. A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis.,Bhabha G, Lee J, Ekiert DC, Gam J, Wilson IA, Dyson HJ, Benkovic SJ, Wright PE Science. 2011 Apr 8;332(6026):234-8. PMID:21474759 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dihydrofolate reductase 3D structures

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