1GN1

crystal structure of the mouse CCT gamma apical domain (monoclinic)

1GN1 の概要

• エントリーDOI: 10.2210/pdb1gn1/pdb
• 関連するPDBエントリー: 1GML
• 分子名称: CCT-GAMMA, CALCIUM ION (3 entities in total)
• 機能のキーワード: chaperone, chaperonin, actin, tubulin
• 由来する生物種: MUS MUSCULUS (MOUSE)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 165237.76

構造登録者

Pappenberger, G.,Wilsher, J.A.,Roe, S.M.,Willison, K.R.,Pearl, L.H. (登録日: 2001-10-01, 公開日: 2002-06-18, 最終更新日: 2024-11-13)

主引用文献

Pappenberger, G.,Wilsher, J.A.,Roe, S.M.,Counsell, D.J.,Willison, K.R.,Pearl, L.H.
Crystal Structure of the Cct Gamma Apical Domain:: Implications for Substrate Binding to the Eukaryotic Cytosolic Chaperonin
J.Mol.Biol., 318:1367-, 2002

PubMed Abstract: The chaperonin containing TCP-1 (CCT, also known as TRiC) is the only member of the chaperonin family found in the cytosol of eukaryotes. Like other chaperonins, it assists the folding of newly synthesised proteins. It is, however, unique in its specificity towards only a small subset of non-native proteins. We determined two crystal structures of mouse CCTgamma apical domain at 2.2 A and 2.8 A resolution. They reveal a surface patch facing the inside of the torus that is highly evolutionarily conserved and specific for the CCTgamma apical domain. This putative substrate-binding region consists of predominantly positively charged side-chains. It suggests that the specificity of this apical domain towards its substrate, partially folded tubulin, is conferred by polar and electrostatic interactions. The site and nature of substrate interaction are thus profoundly different between CCT and its eubacterial homologue GroEL, consistent with their different functions in general versus specific protein folding assistance.

PubMed: 12083524
DOI: 10.1016/S0022-2836(02)00190-0

実験手法

X-RAY DIFFRACTION (2.8 Å)