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)

Abstract

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
• Status: Published
• Refereed: Yes
• 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
• Publisher: Elsevier
• ISSN: 0022-2836
• ISSN (Online): 1089-8638