3DU0

E. coli dihydrodipicolinate synthase with first substrate, pyruvate, bound in active site

3DU0 の概要

• エントリーDOI: 10.2210/pdb3du0/pdb
• 関連するPDBエントリー: 1YXC
• 分子名称: Dihydrodipicolinate synthase, POTASSIUM ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: alpha/beta barrel, tim barrel, lyase, amino-acid biosynthesis, diaminopimelate biosynthesis, lysine biosynthesis, schiff base
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63322.44

構造登録者

Dobson, R.C.J.,Devenish, S.R.A.,Gerrard, J.A.,Jameson, G.B. (登録日: 2008-07-16, 公開日: 2008-11-18, 最終更新日: 2025-03-26)

主引用文献

Devenish, S.R.,Gerrard, J.A.,Jameson, G.B.,Dobson, R.C.
The high-resolution structure of dihydrodipicolinate synthase from Escherichia coli bound to its first substrate, pyruvate.
Acta Crystallogr.,Sect.F, 64:1092-1095, 2008

PubMed Abstract: Dihydrodipicolinate synthase (DHDPS) mediates the key first reaction common to the biosynthesis of (S)-lysine and meso-diaminopimelate, molecules which play a crucial cross-linking role in bacterial cell walls. An effective inhibitor of DHDPS would represent a useful antibacterial agent; despite extensive effort, a suitable inhibitor has yet to be found. In an attempt to examine the specificity of the active site of DHDPS, the enzyme was cocrystallized with the substrate analogue oxaloacetate. The resulting crystals diffracted to 2.0 A resolution, but solution of the protein structure revealed that pyruvate was bound in the active site rather than oxaloacetic acid. Kinetic analysis confirmed that the decarboxylation of oxaloacetate was not catalysed by DHDPS and was instead a slow spontaneous chemical process.

PubMed: 19052357
DOI: 10.1107/S1744309108033654

実験手法

X-RAY DIFFRACTION (2 Å)