1qsd
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(New page: 200px<br /><applet load="1qsd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qsd, resolution 2.2Å" /> '''RBL2P, BETA-TUBULIN B...)
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Revision as of 22:49, 20 November 2007
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RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR
Overview
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.
About this Structure
1QSD is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of the post-chaperonin beta-tubulin binding cofactor Rbl2p., Steinbacher S, Nat Struct Biol. 1999 Nov;6(11):1029-32. PMID:10542094
Page seeded by OCA on Wed Nov 21 00:56:34 2007
