2YXG

Crystal structure of Dihyrodipicolinate Synthase (dapA)

2YXG の概要

• エントリーDOI: 10.2210/pdb2yxg/pdb
• 分子名称: Dihydrodipicolinate synthase (2 entities in total)
• 機能のキーワード: mj0244, dihydrodipicolinate synthase, tim beta/alpha-barrel fold, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, lyase
• 由来する生物種: Methanocaldococcus jannaschii DSM 2661
• 細胞内の位置: Cytoplasm (By similarity): Q57695
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 126453.74

構造登録者

Padmanabhan, B.,Bessho, Y.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2007-04-26, 公開日: 2007-10-30, 最終更新日: 2023-10-25)

主引用文献

Padmanabhan, B.,Strange, R.W.,Antonyuk, S.V.,Ellis, M.J.,Hasnain, S.S.,Iino, H.,Agari, Y.,Bessho, Y.,Yokoyama, S.
Structure of dihydrodipicolinate synthase from Methanocaldococcus jannaschii.
Acta Crystallogr.,Sect.F, 65:1222-1226, 2009

PubMed Abstract: In bacteria and plants, dihydrodipicolinate synthase (DHDPS) plays a key role in the (S)-lysine biosynthesis pathway. DHDPS catalyzes the first step of the condensation of (S)-aspartate-beta-semialdehyde and pyruvate to form an unstable compound, (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid. The activity of DHDPS is allosterically regulated by (S)-lysine, a feedback inhibitor. The crystal structure of DHDPS from Methanocaldococcus jannaschii (MjDHDPS) was solved by the molecular-replacement method and was refined to 2.2 A resolution. The structure revealed that MjDHDPS forms a functional homotetramer, as also observed in Escherichia coli DHDPS, Thermotoga maritima DHDPS and Bacillus anthracis DHDPS. The binding-site region of MjDHDPS is essentially similar to those found in other known DHDPS structures.

PubMed: 20054116
DOI: 10.1107/S174430910904651X

実験手法

X-RAY DIFFRACTION (2.2 Å)