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Lookup NU author(s): Professor Alastair Hawkins
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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 Å. 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°. Detailed knowledge of shikimate binding is an important step in the design of inhibitors of SK, which have potential as novel anti-tuberculosis agents. © 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Author(s): Dhaliwal B, Nichols CE, Ren J, Lockyer M, Charles I, Hawkins AR, Stammers DK
Publication type: Article
Publication status: Published
Journal: FEBS Letters
ISSN (print): 0014-5793
ISSN (electronic): 1873-3468
Publisher: Elsevier BV
PubMed id: 15358538
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