Work

Using neutron protein crystallography to understand enzyme mechanisms

Year: 2010

Type: article

Abstract: A description is given of the results of neutron diffraction studies of the structures of four different metal-ion complexes of deuterated D-xylose isomerase. These represent four stages in the progression of the biochemical catalytic action of this enzyme. Analyses of the structural changes observed between the various three-dimensional structures lead to some insight into the mechanism of action of this enzyme.

Source: Acta Crystallographica Section D Biological Crystallography

DOI: 10.1107/s0907444910027915

Authors: Jenny P. Glusker, H. L. Carrell, Andrey Y. Kovalevsky, Leif Hanson, S. Zoe Fisher, Marat Mustyakimov, Sax Mason, Trevor Forsyth, Paul Langan

Institutions: Fox Chase Cancer Center, Los Alamos National Laboratory, University of Toledo, Institut Laue-Langevin

Language: English

Topic: Enzyme Structure and Function

Subfield: Structural Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Cancer Institute, National Institute of General Medical Sciences

Awards: APPLICATION OF CRYSTALLOGRAPHIC TECHNIQUES, Computational Tools for Neutron Protein Crystallography, Comprehensive Cancer Center Program at Fox Chase

OpenAlex ID: W2073206318

FWCI: 0.47

Cites: 6

Cited by: 7

Related to: 10