2NWC

A 3.02 angstrom crystal structure of wild-type apo GroEL in a monoclinic space group

2NWC の概要

• エントリーDOI: 10.2210/pdb2nwc/pdb
• 分子名称: 60 kDa chaperonin (1 entity in total)
• 機能のキーワード: chaperonin, hsp60, chaperone
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm (By similarity): Q1R3B6
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 801647.06

構造登録者

Kiser, P.D.,Lodowski, D.T.,Palczewski, K. (登録日: 2006-11-14, 公開日: 2007-05-22, 最終更新日: 2023-08-30)

主引用文献

Kiser, P.D.,Lodowski, D.T.,Palczewski, K.
Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions
Acta Crystallogr.,Sect.F, 63:457-461, 2007

PubMed Abstract: GroEL is a member of the ATP-dependent chaperonin family that promotes the proper folding of many cytosolic bacterial proteins. The structures of GroEL in a variety of different states have been determined using X-ray crystallography and cryo-electron microscopy. In this study, a 3.02 A crystal structure of the native GroEL complex from Escherichia coli is presented. The complex was purified and crystallized in the absence of potassium ions, which allowed evaluation of the structural changes that may occur in response to cognate potassium-ion binding by comparison to the previously determined wild-type GroEL structure (PDB code 1xck), in which potassium ions were observed in all 14 subunits. In general, the structure is similar to the previously determined wild-type GroEL crystal structure with some differences in regard to temperature-factor distribution.

PubMed: 17554162
DOI: 10.1107/S1744309107020295

実験手法

X-RAY DIFFRACTION (3.02 Å)