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The Reaction Coordinate of a Bacterial GH47 α-Mannosidase: A Combined Quantum Mechanical and Structural Approach
DOI:
10.1002/anie.201205338
PMID:
23012075
Authors:
Andrew J.
Thompson
(University of York)
,
Jerome
Dabin
(University of York)
,
Javier
Iglesias-fernández
(Parc Científic de Barcelona)
,
Albert
Ardèvol
(Parc Científic de Barcelona)
,
Zoran
Dinev
(University of Melbourne)
,
Spencer J.
Williams
(University of Melbourne)
,
Omprakash
Bande
(Université de Picardie Jules Vernes)
,
Aloysius
Siriwardena
(Université de Picardie Jules Vernes)
,
Carl
Moreland
(Newcastle University)
,
Ting-chou
Hu
(University of York)
,
David K.
Smith
(University of York)
,
Harry J.
Gilbert
(Newcastle University)
,
Carme
Rovira
(University of York)
,
Gideon J.
Davies
(University of York)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Angewandte Chemie International Edition
, VOL 51 (44)
, PAGES 10997 - 11001
State:
Published (Approved)
Published:
October 2012

Abstract: Mannosides in the southern hemisphere: Conformational analysis of enzymatic mannoside hydrolysis informs strategies for enzyme inhibition and inspires solutions to mannoside synthesis. Atomic resolution structures along the reaction coordinate of an inverting α-mannosidase show how the enzyme distorts the substrate and transition state. QM/MM calculations reveal how the free energy landscape of isolated α-D-mannose is molded on enzyme to only allow one conformationally accessible reaction coordinate.
Journal Keywords: Caulobacter; Protein; Quantum; alpha-Mannosidase
Subject Areas:
Chemistry
Instruments:
I03-Macromolecular Crystallography
,
I04-1-Macromolecular Crystallography (fixed wavelength)
,
I04-Macromolecular Crystallography
Added On:
24/09/2015 14:55
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