Structural highlights
Function
[TBCA_YEAST] Tubulin-folding protein; involved in the early step of the tubulin folding pathway.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of the post-chaperonin beta-tubulin binding cofactor Rbl2p.,Steinbacher S Nat Struct Biol. 1999 Nov;6(11):1029-32. PMID:10542094[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Steinbacher S. Crystal structure of the post-chaperonin beta-tubulin binding cofactor Rbl2p. Nat Struct Biol. 1999 Nov;6(11):1029-32. PMID:10542094 doi:10.1038/14912
