2iyy

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

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 ... [(full description)]

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]. Structure known Active 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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