1IOK

CRYSTAL STRUCTURE OF CHAPERONIN-60 FROM PARACOCCUS DENITRIFICANS

1IOK の概要

• エントリーDOI: 10.2210/pdb1iok/pdb
• 分子名称: CHAPERONIN 60 (1 entity in total)
• 機能のキーワード: chaperonin, chaperone
• 由来する生物種: Paracoccus denitrificans
• 細胞内の位置: Cytoplasm (By similarity): Q9Z462
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 404515.86

構造登録者

Fukami, T.A.,Yohda, M.,Taguchi, H.,Yoshida, M.,Miki, K. (登録日: 2001-03-16, 公開日: 2001-10-03, 最終更新日: 2023-12-27)

主引用文献

Fukami, T.A.,Yohda, M.,Taguchi, H.,Yoshida, M.,Miki, K.
Crystal structure of chaperonin-60 from Paracoccus denitrificans.
J.Mol.Biol., 312:501-509, 2001

PubMed Abstract: The crystal structure of chaperonin-60 from Paracoccus denitrificans (P.cpn60) has been determined at 3.2 A resolution by the molecular replacement method. Two heptameric rings of identical subunits of P.cpn60 in adjacent asymmetric units are stacked in a back-to-back manner and form a cylinder, as found in GroEL, cpn60 from Escherichia coli. With respect to the unliganded GroEL structure, each subunit of P.cpn60 tilts 2 degrees outwards and the apical domain twists 4 degrees counter-clockwise in the top view in a hinge-like manner, rendering the central hole 5 A wider. Despite the subunit tilts, both rings in P.cpn60 contact at two sites of the equatorial domain in the same way as in GroEL. Interactions between residues 434 and 434, and 463 and 463 observed in GroEL were not found in P.cpn60, and the interaction between 452 and 461 was weaker in P.cpn60 than in GroEL. The unique hydrogen bond between 468 and 471 was observed at the right site in P.cpn60, which could account for why the subunits tilt outwards. The contact surface area was reduced at the left site, which is similar to the observed changes in the GroEL structures induced by ATP binding. In general, inter-ring interactions in P.cpn60 were weakened, which is consistent with findings that P.cpn60 is observed in single-ring forms as well as in double-ring forms.

PubMed: 11563912
DOI: 10.1006/jmbi.2001.4961

実験手法

X-RAY DIFFRACTION (3.2 Å)