1QSD

RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR

Summary for 1QSD

Entry DOI	10.2210/pdb1qsd/pdb
Descriptor	PROTEIN (BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR) (2 entities in total)
Functional Keywords	four-helix-bundle, chaperone
Biological source	Saccharomyces cerevisiae (baker's yeast)
Cellular location	Cytoplasm, cytoskeleton: P48606
Total number of polymer chains	2
Total formula weight	24797.93
Authors	Steinbacher, S. (deposition date: 1999-06-21, release date: 1999-12-22, Last modification date: 2024-02-14)
Primary citation	Steinbacher, S. Crystal structure of the post-chaperonin beta-tubulin binding cofactor Rbl2p Nat.Struct.Biol., 6:1029-1032, 1999 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation