1TE6

Crystal Structure of Human Neuron Specific Enolase at 1.8 angstrom

1TE6 の概要

• エントリーDOI: 10.2210/pdb1te6/pdb
• 分子名称: Gamma enolase, MAGNESIUM ION, PHOSPHATE ION, ... (6 entities in total)
• 機能のキーワード: enolase, neurons, isozymes, surface charges, negative cooperativity, lyase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (By similarity): P09104
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96361.64

構造登録者

Chai, G.,Brewer, J.,Lovelace, L.,Aoki, T.,Minor, W.,Lebioda, L. (登録日: 2004-05-24, 公開日: 2004-09-21, 最終更新日: 2023-08-23)

主引用文献

Chai, G.,Brewer, J.,Lovelace, L.,Aoki, T.,Minor, W.,Lebioda, L.
Expression, Purification and the 1.8 A Resolution Crystal Structure of Human Neuron Specific Enolase
J.Mol.Biol., 341:1015-1021, 2004

PubMed Abstract: Human neuron-specific enolase (NSE) or isozyme gamma has been expressed with a C-terminal His-tag in Escherichia coli. The enzyme has been purified, crystallized and its crystal structure determined. In the crystals the enzyme forms the asymmetric complex NSE x Mg2 x SO4/NSE x Mg x Cl, where "/" separates the dimer subunits. The subunit that contains the sulfate (or phosphate) ion and two magnesium ions is in the closed conformation observed in enolase complexes with the substrate or its analogues; the other subunit is in the open conformation observed in enolase subunits without bound substrate or analogues. This indicates negative cooperativity for ligand binding between subunits. Electrostatic charge differences between isozymes alpha and gamma, -19 at physiological pH, are concentrated in the regions of the molecular surface that are negatively charged in alpha, i.e. surface areas negatively charged in alpha are more negatively charged in gamma, while areas that are neutral or positively charged tend to be charge-conserved.

PubMed: 15289101
DOI: 10.1016/j.jmb.2004.05.068

実験手法

X-RAY DIFFRACTION (1.8 Å)