4QWM

KINETIC CRYSTALLOGRAPHY of ALPHA_E7-CARBOXYLESTERSE FROM LUCILLA CUPRINA - ABSORBED X-RAY DOSE 1.85 MGy

4QWM の概要

• エントリーDOI: 10.2210/pdb4qwm/pdb
• 分子名称: E3, DIETHYL HYDROGEN PHOSPHATE (3 entities in total)
• 機能のキーワード: alpha/beta hydrolase fold, carboxylesterase, hydrolase
• 由来する生物種: Lucilia cuprina (greenbottle fly)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 65626.88

構造登録者

Jackson, C.J.,Carr, P.D.,Weik, M.,Huber, T.,Meirelles, T.,Correy, G. (登録日: 2014-07-16, 公開日: 2015-07-22, 最終更新日: 2023-11-08)

主引用文献

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

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: 27210287
DOI: 10.1016/j.str.2016.04.009

実験手法

X-RAY DIFFRACTION (2.17 Å)