3B97

Crystal Structure of human Enolase 1

3B97 の概要

• エントリーDOI: 10.2210/pdb3b97/pdb
• 分子名称: Alpha-enolase, MAGNESIUM ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: alpha/beta hydrolase, acetylation, alternative initiation, cytoplasm, dna-binding, glycolysis, lyase, magnesium, membrane, metal-binding, nucleus, phosphorylation, plasminogen activation, polymorphism, repressor, transcription, transcription regulation
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm. Isoform MBP-1: Nucleus: P06733
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 188973.35

構造登録者

Kang, H.J.,Jung, S.K.,Kim, S.J.,Chung, S.J. (登録日: 2007-11-02, 公開日: 2008-09-16, 最終更新日: 2024-03-13)

主引用文献

Kang, H.J.,Jung, S.K.,Kim, S.J.,Chung, S.J.
Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme.
Acta Crystallogr.,Sect.D, 64:651-657, 2008

PubMed Abstract: Aside from its enzymatic function in the glycolytic pathway, alpha-enolase (ENO1) has been implicated in numerous diseases, including metastatic cancer, autoimmune disorders, ischaemia and bacterial infection. The disease-related roles of ENO1 are mostly attributed to its immunogenic capacity, DNA-binding ability and plasmin(ogen) receptor function, which are significantly affected by its three-dimensional structure and surface properties, rather than its enzymatic activity. Here, the crystal structure of human ENO1 (hENO1) is presented at 2.2 A resolution. Despite its high sequence similarity to other enolases, the hENO1 structure exhibits distinct surface properties, explaining its various activities, including plasmin(ogen) and DNA binding.

PubMed: 18560153
DOI: 10.1107/S0907444908008561

実験手法

X-RAY DIFFRACTION (2.2 Å)