2iyy | pdb_00002iyy

File:2iyy.gif

spinqualitylabelsall models 2iyy, resolution 1.62Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND SO4

Overview

The structural mechanism of the catalytic functioning of shikimate kinase from Mycobacterium tuberculosis was investigated on the basis of a series of high-resolution crystal structures corresponding to individual steps in the enzymatic reaction. The catalytic turnover of shikimate and ATP into the products shikimate-3-phosphate and ADP, followed by release of ADP, was studied in the crystalline environment. Based on a comparison of the structural states before initiation of the reaction and immediately after the catalytic step, we derived a structural model of the transition state that suggests that phosphoryl transfer proceeds with inversion by an in-line associative mechanism. The random sequential binding of shikimate and nucleotides is associated with domain movements. We identified a synergic mechanism by which binding of the first substrate may enhance the affinity for the second substrate.

About this Structure

2IYY is a Single protein structure of sequence from Mycobacterium tuberculosis with SO4, PO4, MG, CL and S3P as ligands. Active as Shikimate kinase, with EC number 2.7.1.71 Known structural/functional Site: AC1. Full crystallographic information is available from OCA.

Reference

Mechanism of phosphoryl transfer catalyzed by shikimate kinase from Mycobacterium tuberculosis., Hartmann MD, Bourenkov GP, Oberschall A, Strizhov N, Bartunik HD, J Mol Biol. 2006 Dec 1;364(3):411-23. Epub 2006 Sep 5. PMID:17020768

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