4AYR

Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with noeuromycin

Summary for 4AYR

• Entry DOI: 10.2210/pdb4ayr/pdb
• Related: 4AYO 4AYP 4AYQ
• Descriptor: MANNOSYL-OLIGOSACCHARIDE 1,2-ALPHA-MANNOSIDASE, CALCIUM ION, SODIUM ION, ... (6 entities in total)
• Functional Keywords: hydrolase, gh47, cazy, enzyme-carbohydrate interaction, mannose, glycosidase inhibition
• Biological source: CAULOBACTER SP.
• Total number of polymer chains: 1
• Total formula weight: 52744.31

Authors

Thompson, A.J.,Dabin, J.,Iglesias-Fernandez, J.,Iglesias-Fernandez, A.,Dinev, Z.,Williams, S.J.,Siriwardena, A.,Moreland, C.,Hu, T.C.,Smith, D.K.,Gilbert, H.J.,Rovira, C.,Davies, G.J. (deposition date: 2012-06-21, release date: 2013-01-30, Last modification date: 2023-12-20)

Primary citation

Thompson, A.J.,Dabin, J.,Iglesias-Fernandez, J.,Ardevol, A.,Dinev, Z.,Williams, S.J.,Bande, O.,Siriwardena, A.,Moreland, C.,Hu, T.C.,Smith, D.K.,Gilbert, H.J.,Rovira, C.,Davies, G.J.
The Reaction Coordinate of a Bacterial Gh47 Alpha-Mannosidase: A Combined Quantum Mechanical and Structural Approach.
Angew.Chem.Int.Ed.Engl., 51:10997-, 2012

PubMed 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.

PubMed: 23012075
DOI: 10.1002/ANIE.201205338

Experimental method

X-RAY DIFFRACTION (1.1 Å)