The three-dimensional structure of shikimate kinase

Krell, T., Coggins, J. R. and Lapthorn, A. J. (1998) The three-dimensional structure of shikimate kinase. Journal of Molecular Biology, 278(5), pp. 983-997. (doi: 10.1006/jmbi.1998.1755) (PMID:9600856)

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The three-dimensional structure of shikimate kinase from Erwinia chrysanthemi has been determined by multiple isomorphous replacement. Two models are presented: a high resolution 1.9 Å model and a 2.6 Å model which contains bound Mg-ADP. The enzyme is an α/β protein consisting of a central sheet of five parallel β-strands flanked by α-helices with overall topology similar to adenylate kinase. Evidence is presented that shikimate kinase undergoes major conformational changes on ligand binding. It resembles adenylate kinase in having a P-loop containing core structure and two flexible domains which undergo induced fit movement on substrate binding. The binding of Mg2+ in the active site of shikimate kinase involves direct interaction with two protein side-chains which is different from the situation found in adenylate kinase. Shikimate kinase has a readily identifiable Walker A-motif and a recognisable but modified Walker B-motif. Comparison of shikimate kinase to adenylate kinase has led to the identification of an adenine-binding motif (I/VDAXQ/NXP). Difference Fourier calculations have revealed the shikimate binding site which corresponds to the location of the AMP-binding site in adenylate kinase. A model for shikimate-binding is presented.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Lapthorn, Dr Adrian and Coggins, Professor John
Authors: Krell, T., Coggins, J. R., and Lapthorn, A. J.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Journal of Molecular Biology
ISSN (Online):1089-8638

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