PDBsum entry 5ivd

Hydrolase

PDB id: 5ivd

Contents

Protein chain

566 a.a.

Waters ×274

PDB id:

5ivd

Name:

Hydrolase

Title:

The alpha-esterase-7 carboxylesterase, e3, from the blowfly lucilia cuprina: apo-enzyme qfit multi-conformer model

Structure:

Carboxylic ester hydrolase. Chain: a. Engineered: yes

Source:

Lucilia cuprina. Green bottle fly. Organism_taxid: 7375. Gene: lcae7. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.71Å R-factor: 0.180 R-free: 0.230

Authors:

G.J.Correy,C.J.Jackson

Key ref:

G.J.Correy et al. (2016). Mapping the Accessible Conformational Landscape of an Insect Carboxylesterase Using Conformational Ensemble Analysis and Kinetic Crystallography. Structure, 24, 977-987. PubMed id: 27210287 DOI: 10.1016/j.str.2016.04.009

Date:

20-Mar-16 Release date: 15-Jun-16

Protein chain

Q25252  (Q25252_LUCCU) -  Carboxylic ester hydrolase from Lucilia cuprina

Seq: 570 a.a.

Struc: 566 a.a.*

* PDB and UniProt seqs differ at 7 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.1.1.- - ?????

DOI no: 10.1016/j.str.2016.04.009

Structure 24:977-987 (2016)

PubMed id: 27210287

Mapping the Accessible Conformational Landscape of an Insect Carboxylesterase Using Conformational Ensemble Analysis and Kinetic Crystallography.

G.J.Correy, P.D.Carr, T.Meirelles, P.D.Mabbitt, N.J.Fraser, M.Weik, C.J.Jackson.

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.