5CH5: E3 Alpha-esterase-7 Carboxylesterase

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 (LcalphaE7) as it traverses all steps in its catalytic cycle. LcalphaE7 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.
PDB ID: 5CH5Download
MMDB ID: 140056
PDB Deposition Date: 2015/7/10
Updated in MMDB: 2016/06
Experimental Method:
x-ray diffraction
Resolution: 1.53  Å
Source Organism:
Similar Structures:
Biological Unit for 5CH5: monomeric; determined by author and by software (PISA)
Molecular Components in 5CH5
Label Count Molecule
Protein (1 molecule)
Carboxylic Ester Hydrolase
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB