2CGT

GROEL-ADP-gp31 COMPLEX

2CGT の概要

• エントリーDOI: 10.2210/pdb2cgt/pdb
• 関連するPDBエントリー: 1AON 1DK7 1DKD 1FY9 1FYA 1G31 1GR5 1GRL 1GRU 1J4Z 1JON 1KID 1KP8 1KPO 1LA1 1MNF 1OEL 1PCQ 1PF9 1SS8 1SVT 1SX3 1SX4 1XCK 2C7C 2C7D 2C7E
• EMDBエントリー: 1202
• 分子名称: 60 KDA GROEL, CAPSID ASSEMBLY PROTEIN GP31 (2 entities in total)
• 機能のキーワード: chaperonin, chaperone, cell cycle, cell division, capsid assembly, early protein
• 由来する生物種: ESCHERICHIA COLI; 詳細
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 886291.05

構造登録者

Clare, D.K.,Bakkes, P.J.,van Heerikhuizen, H.,van der Vies, S.M.,Saibil, H.R. (登録日: 2006-03-09, 公開日: 2006-03-29, 最終更新日: 2024-05-08)

主引用文献

Clare, D.K.,Bakkes, P.J.,Van Heerikhuizen, H.,Van Der Vies, S.M.,Saibil, H.R.
An Expanded Protein Folding Cage in the Groel-Gp31 Complex.
J.Mol.Biol., 358:905-, 2006

PubMed Abstract: Bacteriophage T4 produces a GroES analogue, gp31, which cooperates with the Escherichia coli GroEL to fold its major coat protein gp23. We have used cryo-electron microscopy and image processing to obtain three-dimensional structures of the E.coli chaperonin GroEL complexed with gp31, in the presence of both ATP and ADP. The GroEL-gp31-ADP map has a resolution of 8.2 A, which allows accurate fitting of the GroEL and gp31 crystal structures. Comparison of this fitted structure with that of the GroEL-GroES-ADP structure previously determined by cryo-electron microscopy shows that the folding cage is expanded. The enlarged volume for folding is consistent with the size of the bacteriophage coat protein gp23, which is the major substrate of GroEL-gp31 chaperonin complex. At 56 kDa, gp23 is close to the maximum size limit of a polypeptide that is thought to fit inside the GroEL-GroES folding cage.

PubMed: 16549073
DOI: 10.1016/J.JMB.2006.02.033

実験手法

ELECTRON MICROSCOPY (8.2 Å)