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Crystal structure of the post-chaperonin β-tubulin binding cofactor Rbl2p

Nature Structural Biology volume 6, pages 1029–1032 (1999)Cite this article

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 Å crystal structure of Rbl2p, the Saccharomyces cerevisiae homolog of β-tubulin specific cofactor A, shows α-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.

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Figure 1: Electron density.
Figure 2: Stereo diagrams of Rbl2p.
Figure 3: Secondary structure of Rbl2p and sequence comparison to mammalian cofactor A sequences.
Figure 4: Surface properties of Rbl2p.

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Acknowledgements

The author thanks Robert Huber for his generous support. The work was financially supported by the Deutsche Forschungsgemeinschaft.

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  1. Abteilung Strukturforschung, Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, Martinsried, 82152, Germany

    Stefan Steinbacher

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  1. Stefan Steinbacher
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Correspondence to Stefan Steinbacher.

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Steinbacher, S. Crystal structure of the post-chaperonin β-tubulin binding cofactor Rbl2p. Nat Struct Mol Biol 6, 1029–1032 (1999). https://doi.org/10.1038/14912

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