1IYX

Crystal structure of enolase from Enterococcus hirae

1IYX の概要

• エントリーDOI: 10.2210/pdb1iyx/pdb
• 分子名称: ENOLASE, MAGNESIUM ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: enolase family, lyase
• 由来する生物種: Enterococcus hirae
• 細胞内の位置: Cytoplasm: Q8GR70
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93705.53

構造登録者

Hosaka, T.,Meguro, T.,Yamato, I.,Shirakihara, Y. (登録日: 2002-09-12, 公開日: 2003-07-29, 最終更新日: 2023-10-25)

主引用文献

Hosaka, T.,Meguro, T.,Yamato, I.,Shirakihara, Y.
Crystal Structure of Enterococcus hirae Enolase at 2.8 A Resolution
J.BIOCHEM.(TOKYO), 133:817-823, 2003

PubMed Abstract: We report the crystal structure of an enolase from Enterococcus hirae, which is the first report of a structure determination among gram-positive bacteria. We isolated the enolase gene and determined the base sequence. The amino acid sequence deduced from the DNA sequence suggests that this enolase is composed of 431 amino acids. The amino acid sequence is very similar to those of enolases from eukaryotic and prokaryotic organisms, being 65% and 50% identical to enolases from Escherichia coli and yeast, respectively. The enolase prepared from E. hirae lysate yielded crystals containing one dimer per asymmetric unit. X-ray diffraction patterns were obtained at 2.8 A resolution on a SPring-8 synchrotron radiation source. Crystals belong to space group I4 with unit cell dimensions of a = b = 153.5 A, c = 90.7 A. The E. hirae, yeast, E. coli and lobster enolase structures are very similar. The E. hirae enolase takes an "Open" conformation. The regions in the structure that differ most from other enolases are loops L4 (132-140) and L3 (244-265). Considering the positions of these loops relative to the active site, they seem to have no direct involvement in function. Our findings show that the three dimensional structure of an important enzyme in the glycolytic pathway is evolutionarily conserved among eukaryotes and prokaryotes, including gram-positive bacteria.

PubMed: 12869539
DOI: 10.1093/jb/mvg104

実験手法

X-RAY DIFFRACTION (2.8 Å)