1u8a

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{{STRUCTURE_1u8a| PDB=1u8a | SCENE= }}
{{STRUCTURE_1u8a| PDB=1u8a | SCENE= }}
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'''Crystal Structure of Mycobacterium Tuberculosis Shikimate Kinase in Complex with Shikimate and ADP at 2.15 Angstrom Resolution'''
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===Crystal Structure of Mycobacterium Tuberculosis Shikimate Kinase in Complex with Shikimate and ADP at 2.15 Angstrom Resolution===
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==Overview==
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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 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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15358538 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15358538}}
==About this Structure==
==About this Structure==
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[[Category: Shikimate pathway]]
[[Category: Shikimate pathway]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:53:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:41:15 2008''

Revision as of 01:41, 29 July 2008

Template:STRUCTURE 1u8a

Crystal Structure of Mycobacterium Tuberculosis Shikimate Kinase in Complex with Shikimate and ADP at 2.15 Angstrom Resolution

Template:ABSTRACT PUBMED 15358538

About this Structure

1U8A is a Single protein structure of sequence from Mycobacterium tuberculosis. 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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