1t0y

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Revision as of 00:47, 21 November 2007

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Solution Structure of a Ubiquitin-Like Domain from Tubulin-binding Cofactor B

Overview

Proper folding and assembly of tubulin alphabeta-heterodimers involves a, stepwise progression mediated by a group of protein cofactors A through E., Upon release of the tubulin monomers from the chaperonin CCT, they are, acted upon by each cofactor in the folding pathway through a unique, combination of protein interaction domains. Three-dimensional structures, have previously been reported for cofactor A and the C-terminal CAP-Gly, domain of cofactor B (CoB). Here we report the NMR structure of the, N-terminal domain of Caenorhabditis elegans CoB and show that it closely, resembles ubiquitin as was recently postulated on the basis of, bioinformatic analysis (Grynberg, M., Jaroszewski, L., and Godzik, A., (2003) BMC Bioinformatics 4, 46). CoB binds partially folded alpha-tubulin, monomers, and a putative tubulin-binding motif within the N-terminal, domain is identified from sequence and structure comparisons. Based on, modeling of the homologous cofactor E ubiquitin-like domain, we, hypothesize that cofactors B and E may associate via their beta-grasp, domains in a manner analogous to the PB1 and caspase-activated, deoxyribonuclease superfamily of protein interaction domains.

About this Structure

1T0Y is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.

Reference

Solution structure of a ubiquitin-like domain from tubulin-binding cofactor B., Lytle BL, Peterson FC, Qiu SH, Luo M, Zhao Q, Markley JL, Volkman BF, J Biol Chem. 2004 Nov 5;279(45):46787-93. Epub 2004 Sep 9. PMID:15364906

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