1U8A

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

1U8A の概要

• エントリーDOI: 10.2210/pdb1u8a/pdb
• 関連するPDBエントリー: 1L4U 1L4Y
• 分子名称: Shikimate kinase, CHLORIDE ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: shikimate pathway, shikimate kinase, 2 phorsphoryl transfer, drug design, transferase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19320.06

構造登録者

Dhaliwal, B.,Nichols, C.E.,Ren, J.,Lockyer, M.,Charles, I.,Hawkins, A.R.,Stammers, D.K. (登録日: 2004-08-05, 公開日: 2004-10-19, 最終更新日: 2023-08-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.15 Å)