1LEP

THREE-DIMENSIONAL STRUCTURE OF THE IMMUNODOMINANT HEAT-SHOCK PROTEIN CHAPERONIN-10 OF MYCOBACTERIUM LEPRAE

1LEP の概要

• エントリーDOI: 10.2210/pdb1lep/pdb
• 分子名称: CHAPERONIN-10 (1 entity in total)
• 機能のキーワード: chaperone, antigen, heat shock
• 由来する生物種: Mycobacterium leprae
• 細胞内の位置: Cytoplasm: P24301
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 74775.05

構造登録者

Mande, S.C.,Hol, W.G.J. (登録日: 1995-12-13, 公開日: 1997-01-11, 最終更新日: 2024-02-14)

主引用文献

Mande, S.C.,Mehra, V.,Bloom, B.R.,Hol, W.G.
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae.
Science, 271:203-207, 1996

PubMed Abstract: Members of the chaperonin-10 (cpn10) protein family, also called heat shock protein 10 and in Escherichia coli GroES, play an important role in ensuring the proper folding of many proteins. The crystal structure of the Mycobacterium leprae cpn10 (Ml-cpn10) oligomer has been elucidated at a resolution of 3.5 angstroms. The architecture of the Ml-cpn10 heptamer resembles a dome with an oculus in its roof. The inner surface of the dome is hydrophilic and highly charged. A flexible region, known to interact with cpn60, extends from the lower rim of the dome. With the structure of a cpn10 heptamer now revealed and the structure of the E. coli GroEL previously known, models of cpn10:cpn60 and GroEL:GroES complexes are proposed.

PubMed: 8539620

実験手法

X-RAY DIFFRACTION (3.5 Å)