3QL3
Re-refined coordinates for PDB entry 1RX2
Summary for 3QL3
| Entry DOI | 10.2210/pdb3ql3/pdb |
| Related | 3QL0 |
| Descriptor | Dihydrofolate reductase, FOLIC ACID, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total) |
| Functional Keywords | rossmann fold, dihydrofolate, tetrahydrofolate, nadph, cofactor, oxidoreductase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 19315.00 |
| Authors | Bhabha, G.,Ekiert, D.C.,Wright, P.E.,Wilson, I.A. (deposition date: 2011-02-02, release date: 2011-04-27, Last modification date: 2024-02-21) |
| Primary citation | Bhabha, G.,Lee, J.,Ekiert, D.C.,Gam, J.,Wilson, I.A.,Dyson, H.J.,Benkovic, S.J.,Wright, P.E. A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis. Science, 332:234-238, 2011 Cited by PubMed Abstract: 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. PubMed: 21474759DOI: 10.1126/science.1198542 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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