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Solution structure of a ubiquitin-like domain from tubulin-binding cofactor B. J Biol Chem 2004 Nov 05;279(45):46787-93 PMID: 15364906


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.

Author List

Lytle BL, Peterson FC, Qiu SH, Luo M, Zhao Q, Markley JL, Volkman BF


Francis C. Peterson PhD Professor in the Biochemistry department at Medical College of Wisconsin
Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Cloning, Molecular
Escherichia coli
Magnetic Resonance Spectroscopy
Microtubule-Associated Proteins
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Conformation
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins
Sequence Homology, Amino Acid

View this publication's entry at the Pubmed website PMID: 15364906
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