4UBN
KINETIC CRYSTALLOGRAPHY OF ALPHA_E7-CARBOXYLESTERSE FROM LUCILLA CUPRINA - ABSORBED X-RAY DOSE 1.85 MGy TEMP 150K
Summary for 4UBN
| Entry DOI | 10.2210/pdb4ubn/pdb |
| Descriptor | E3, DIETHYL HYDROGEN PHOSPHATE (3 entities in total) |
| Functional Keywords | alpha/beta hydrolase fold, carboxylesterase, hydrolase |
| Biological source | Lucilia cuprina (Green bottle fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 65626.88 |
| Authors | Jackson, C.J.,Carr, P.D.,Weik, M.,Huber, T.,Meirelles, T.,Correy, G. (deposition date: 2014-08-13, release date: 2015-08-19, Last modification date: 2023-11-08) |
| Primary citation | Correy, G.J.,Carr, P.D.,Meirelles, T.,Mabbitt, P.D.,Fraser, N.J.,Weik, M.,Jackson, C.J. Mapping the Accessible Conformational Landscape of an Insect Carboxylesterase Using Conformational Ensemble Analysis and Kinetic Crystallography Structure, 24:977-987, 2016 Cited by PubMed Abstract: The proper function of enzymes often depends upon their efficient interconversion between particular conformational sub-states on a free-energy landscape. Experimentally characterizing these sub-states is challenging, which has limited our understanding of the role of protein dynamics in many enzymes. Here, we have used a combination of kinetic crystallography and detailed analysis of crystallographic protein ensembles to map the accessible conformational landscape of an insect carboxylesterase (LcαE7) as it traverses all steps in its catalytic cycle. LcαE7 is of special interest because of its evolving role in organophosphate insecticide resistance. Our results reveal that a dynamically coupled network of residues extends from the substrate-binding site to a surface loop. Interestingly, the coupling of this network that is apparent in the apoenzyme appears to be reduced in the phosphorylated enzyme intermediate. Altogether, the results of this work highlight the importance of protein dynamics to enzyme function and the evolution of new activity. PubMed: 27210287DOI: 10.1016/j.str.2016.04.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.02 Å) |
Structure validation
Download full validation report
