3ENL

REFINED STRUCTURE OF YEAST APO-ENOLASE AT 2.25 ANGSTROMS RESOLUTION

「2ENL」から置き換えられました 「1ENL」から置き換えられました

3ENL の概要

• エントリーDOI: 10.2210/pdb3enl/pdb
• 分子名称: ENOLASE, SULFATE ION (3 entities in total)
• 機能のキーワード: carbon-oxygen lyase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm : P00924
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46786.75

構造登録者

Lebioda, L.,Stec, B. (登録日: 1990-11-13, 公開日: 1992-04-15, 最終更新日: 2024-02-21)

主引用文献

Stec, B.,Lebioda, L.
Refined structure of yeast apo-enolase at 2.25 A resolution.
J.Mol.Biol., 211:235-248, 1990

PubMed Abstract: The crystal structure of apo-enolase from baker's yeast (Saccharomyces cerevisiae) was established at 2.25 A resolution using a restrained least-squares refinement method. Based on 21,077 independent reflections of better than 8 A resolution, a final R-factor of 15.4% was obtained with a model obeying standard geometry within 0.017 A in bond length and 3.5 degrees in bond angles. The upper limit for the co-ordinate accuracy of the atoms was estimated to be 0.18 A. The refinement confirmed the heterodox, non-parallel character of the 8-fold beta alpha-barrel domain with beta beta alpha alpha(beta alpha)6 topology. The reported structure for which the data were collected at pH 5.0 represents an apo-form of the enzyme. Of the three carboxylic ligands that form the conformational metal ion binding site two, Glu295 and Asp320, are very close and presumably form a strong acidic type hydrogen bond with the proton partially replacing the electric charge of the physiological cofactor Mg2+. The single sulfate ion found in the structure is in the active site cavity, co-ordinated to the side-chains of Lys345 and Arg374, and to the N atom of Ser375. It is located about 7.4 A from the conformational metal ion binding site. It occupies the site in which the phosphate group of the substrate binds.

PubMed: 2405163
DOI: 10.1016/0022-2836(90)90023-F

実験手法

X-RAY DIFFRACTION (2.25 Å)