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

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