1L4U

CRYSTAL STRUCTURE OF SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH MGADP AND PT(II) AT 1.8 ANGSTROM RESOLUTION

1L4U の概要

• エントリーDOI: 10.2210/pdb1l4u/pdb
• 関連するPDBエントリー: 1E6C 1L4Y 1SHK 2SHK
• 分子名称: SHIKIMATE KINASE, PLATINUM (II) ION, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: shikimate pathway, shikimate kinase, 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: 19709.96

構造登録者

Gu, Y.,Reshetnikova, L.,Li, Y.,Wu, Y.,Yan, H.,Singh, S.,Ji, X. (登録日: 2002-03-05, 公開日: 2002-06-12, 最終更新日: 2023-08-30)

主引用文献

Gu, Y.,Reshetnikova, L.,Li, Y.,Wu, Y.,Yan, H.,Singh, S.,Ji, X.
Crystal structure of shikimate kinase from Mycobacterium tuberculosis reveals the dynamic role of the LID domain in catalysis.
J.Mol.Biol., 319:779-789, 2002

PubMed Abstract: Shikimate kinase (SK) and other enzymes in the shikimate pathway are potential targets for developing non-toxic antimicrobial agents, herbicides, and anti-parasite drugs, because the pathway is essential in the above species but is absent from mammals. The crystal structure of Mycobacterium tuberculosis SK (MtSK) in complex with MgADP has been determined at 1.8 A resolution, revealing critical information for the structure-based design of novel anti-M. tuberculosis agents. MtSK, with a five-stranded parallel beta-sheet flanked by eight alpha-helices, has three domains: the CORE domain, the shikimate-binding domain (SB), and the LID domain. The ADP molecule is bound with its adenine moiety sandwiched between the side-chains of Arg110 and Pro155, its beta-phosphate group in the P-loop, and the alpha and beta-phosphate groups hydrogen bonded to the guanidinium group of Arg117. Arg117 is located in the LID domain, is strictly conserved in SK sequences, is observed for the first time to interact with any bound nucleotide, and appears to be important in both substrate binding and catalysis. The crystal structure of MtSK (this work) and that of Erwinia chrysanthemi SK suggest a concerted conformational change of the LID and SB domains upon nucleotide binding.

PubMed: 12054870
DOI: 10.1016/S0022-2836(02)00339-X

実験手法

X-RAY DIFFRACTION (1.8 Å)