1QSD

RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR

1QSD の概要

• エントリーDOI: 10.2210/pdb1qsd/pdb
• 分子名称: PROTEIN (BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR) (2 entities in total)
• 機能のキーワード: four-helix-bundle, chaperone
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm, cytoskeleton: P48606
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24797.93

構造登録者

Steinbacher, S. (登録日: 1999-06-21, 公開日: 1999-12-22, 最終更新日: 2024-02-14)

主引用文献

Steinbacher, S.
Crystal structure of the post-chaperonin beta-tubulin binding cofactor Rbl2p
Nat.Struct.Biol., 6:1029-1032, 1999

PubMed Abstract: The folding pathway of tubulins includes highly specific interactions with a series of cofactors (A, B, C, D and E) after they are released from the eukaryotic chaperonin CCT. The 2.2 A crystal structure of Rbl2p, the Saccharomyces cerevisiae homolog of beta-tubulin specific cofactor A, shows alpha-helical monomers forming a flat, slightly convex dimer. The surface of the molecule is dominated by polar and charged residues and lacks hydrophobic patches typically observed for chaperones that bind unfolded or partially folded proteins. This post-chaperonin cofactor is therefore clearly distinct from typical chaperones where hydrophobicity is a hallmark of substrate recognition.

PubMed: 10542094
DOI: 10.1038/14912

実験手法

X-RAY DIFFRACTION (2.2 Å)