3DI1

Crystal structure of the Staphylococcus aureus Dihydrodipicolinate synthase-pyruvate complex

3DI1 の概要

• エントリーDOI: 10.2210/pdb3di1/pdb
• 関連するPDBエントリー: 3DI0
• 分子名称: Dihydrodipicolinate synthase, PYRUVIC ACID (3 entities in total)
• 機能のキーワード: dihydrodipicolinate synthase, lysine biosynthesis, feedback inhibition, ping-pong mechanism, amino-acid biosynthesis, diaminopimelate biosynthesis, lyase, schiff base
• 由来する生物種: Staphylococcus aureus subsp. aureus
• 細胞内の位置: Cytoplasm (By similarity): Q5HG25
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65403.71

構造登録者

Tavarekere, G.S. (登録日: 2008-06-19, 公開日: 2008-08-12, 最終更新日: 2024-10-30)

主引用文献

Girish, T.S.,Sharma, E.,Gopal, B.
Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase
Febs Lett., 582:2923-2930, 2008

PubMed Abstract: Lysine biosynthesis is crucial for cell-wall formation in bacteria. Enzymes involved in lysine biosynthesis are thus potential targets for anti-microbial therapeutics. Dihydrodipicolinate synthase (DHDPS) catalyzes the first step of this pathway. Unlike its homologues, Staphylococcus aureus DHDPS is a dimer both in solution and in the crystal and is not feedback inhibited by lysine. The crystal structure of S. aureus DHDPS in the free and substrate bound forms provides a structural rationale for its catalytic mechanism. The structure also reveals unique conformational features of the S. aureus enzyme that could be crucial for the design of specific non-competitive inhibitors.

PubMed: 18671976
DOI: 10.1016/j.febslet.2008.07.035

実験手法

X-RAY DIFFRACTION (2.2 Å)