6J2L

Crystal structure of Bi-functional enzyme

6J2L の概要

• エントリーDOI: 10.2210/pdb6j2l/pdb
• 分子名称: Histidine biosynthesis bifunctional protein HisIE, ZINC ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: bi-functional enzyme, hydrolase
• 由来する生物種: Shigella flexneri
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45904.85

構造登録者

Zhang, H.,Shang, G.,Wang, Y. (登録日: 2019-01-01, 公開日: 2020-01-01, 最終更新日: 2024-03-27)

主引用文献

Wang, Y.,Zhang, F.,Nie, Y.,Shang, G.,Zhang, H.
Structural analysis of Shigella flexneri bi-functional enzyme HisIE in histidine biosynthesis.
Biochem.Biophys.Res.Commun., 516:540-545, 2019

PubMed Abstract: Histidine biosynthesis, which is absent in animals, was shown to be highly conserved among gram-negative bacteria, thus making it an attractive target for antibiotic design. There are many fusion forms of enzymes in the histidine biosynthetic pathway and people still have limited knowledge about their domain organizations and catalytic mechanisms, due to the lack of structural information. Here we report the first crystal structure of Shigella flexneri bi-functional enzyme HisIE (SfHisIE) that functions in the 2nd and 3rd steps in the histidine biosynthetic pathway. This structure shows that HisIE exists as dimers with two loops (fusion loop) connecting the individual dimer of HisE and HisI in its N-terminus and C-terminus respectively. Our mutagenesis study shows mutations in this fusion loop are lethal for bacteria indicating the advantage of gene fusion in Histidine biosynthesis. Structural analysis revealed several highly conserved residues in the putative ligand binding grooves of HisE and HisI, showing an evolutionarily conserved catalytic mechanism shared among gram negative-bacteria.

PubMed: 31235255
DOI: 10.1016/j.bbrc.2019.06.099

実験手法

X-RAY DIFFRACTION (2.17 Å)