1u8a
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(New page: 200px<br /><applet load="1u8a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u8a, resolution 2.15Å" /> '''Crystal Structure of...)
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Revision as of 01:48, 21 November 2007
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Crystal Structure of Mycobacterium Tuberculosis Shikimate Kinase in Complex with Shikimate and ADP at 2.15 Angstrom Resolution
Overview
The X-ray crystal structure of Mycobacterium tuberculosis shikimate kinase, (SK) with bound shikimate and adenosine diphosphate (ADP) has been, determined to a resolution of 2.15 A. The binding of shikimate in a, shikimate kinase crystal structure has not previously been reported. The, substrate binds in a pocket lined with hydrophobic residues and interacts, with several highly conserved charged residues including Asp34, Arg58, Glu61 and Arg136 which project into the cavity. Comparisons of our ternary, SK-ADP-shikimate complex with an earlier binary SK-ADP complex show that, conformational changes occur on shikimate binding with the, substrate-binding domain rotating by 10 degrees. Detailed knowledge of, shikimate binding is an important step in the design of inhibitors of SK, which have potential as novel anti-tuberculosis agents.
About this Structure
1U8A is a Single protein structure of sequence from Mycobacterium tuberculosis with CL, ADP and SKM as ligands. Active as Shikimate kinase, with EC number 2.7.1.71 Full crystallographic information is available from OCA.
Reference
Crystallographic studies of shikimate binding and induced conformational changes in Mycobacterium tuberculosis shikimate kinase., Dhaliwal B, Nichols CE, Ren J, Lockyer M, Charles I, Hawkins AR, Stammers DK, FEBS Lett. 2004 Sep 10;574(1-3):49-54. PMID:15358538
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