1qsd
From Proteopedia
(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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| - | [[Image:1qsd.gif|left|200px]]<br /><applet load="1qsd" size=" | + | [[Image:1qsd.gif|left|200px]]<br /><applet load="1qsd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qsd, resolution 2.2Å" /> | caption="1qsd, resolution 2.2Å" /> | ||
'''RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR'''<br /> | '''RBL2P, BETA-TUBULIN BINDING POST-CHAPERONIN COFACTOR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The folding pathway of tubulins includes highly specific interactions with | + | 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== | ==About this Structure== | ||
| - | 1QSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 1QSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QSD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: four-helix-bundle]] | [[Category: four-helix-bundle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:18 2008'' |
Revision as of 12:43, 21 February 2008
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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 Thu Feb 21 14:43:18 2008
