1U8A

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

Summary for 1U8A

• Entry DOI: 10.2210/pdb1u8a/pdb
• Related: 1L4U 1L4Y
• Descriptor: Shikimate kinase, CHLORIDE ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: shikimate pathway, shikimate kinase, 2 phorsphoryl transfer, drug design, transferase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 19320.06

Authors

Dhaliwal, B.,Nichols, C.E.,Ren, J.,Lockyer, M.,Charles, I.,Hawkins, A.R.,Stammers, D.K. (deposition date: 2004-08-05, release date: 2004-10-19, Last modification date: 2023-08-23)

Primary citation

Dhaliwal, B.,Nichols, C.E.,Ren, J.,Lockyer, M.,Charles, I.,Hawkins, A.R.,Stammers, D.K.
Crystallographic studies of shikimate binding and induced conformational changes in Mycobacterium tuberculosis shikimate kinase.
Febs Lett., 574:49-54, 2004

PubMed Abstract: 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.

PubMed: 15358538
DOI: 10.1016/j.febslet.2004.08.005

Experimental method

X-RAY DIFFRACTION (2.15 Å)