1zui
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(New page: 200px<br /><applet load="1zui" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zui, resolution 2.300Å" /> '''Structural Basis fo...)
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Revision as of 05:32, 21 November 2007
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Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase
Overview
Shikimate kinase (EC 2.7.1.71) catalyzes the specific phosphorylation of, the 3-hydroxyl group of shikimic acid in the presence of ATP. As the fifth, key step in the shikimate pathway for aromatic amino acid biosynthesis in, bacteria, fungi, and plants, but not mammals, shikimate kinase represents, an attractive target for the development of new antimicrobial agents, herbicides, and antiparasitic agents. Here, we report the 1.8-Angstroms, crystal structure of Helicobacter pylori shikimate kinase (HpSK). The, crystal structure shows a three-layer alpha/beta fold consisting of a, central sheet of five parallel beta-strands flanked by seven, alpha-helices. An HpSK-shikimate-PO(4) complex was also determined and, refined to 2.3 Angstroms, revealing induced-fit movement from an open to a, closed form on substrate binding. Shikimate is located above a short 3(10), helix formed by a strictly conserved motif (GGGXV) after beta(3)., Moreover, several highly conserved charged residues including Asp33 (in a, conserved DT/SD motif), Arg57, and Arg132 (interacting with shikimate) are, identified, guiding the development of novel inhibitors of shikimate, kinase.
About this Structure
1ZUI is a Single protein structure of sequence from Helicobacter pylori with PO4 and SKM as ligands. Active as Shikimate kinase, with EC number 2.7.1.71 Full crystallographic information is available from OCA.
Reference
Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase., Cheng WC, Chang YN, Wang WC, J Bacteriol. 2005 Dec;187(23):8156-63. PMID:16291688
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