1T0Y

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

Summary for 1T0Y

• Entry DOI: 10.2210/pdb1t0y/pdb
• Related: 1LPL
• NMR Information: BMRB: 6176
• Descriptor: tubulin folding cofactor B (1 entity in total)
• Functional Keywords: ubiquitin-like, cytoskeleton, microtubule, tubulin, cesg, structural genomics, protein structure initiative, psi, center for eukaryotic structural genomics, chaperone
• Biological source: Caenorhabditis elegans
• Cellular location: Cytoplasm (By similarity): Q20728
• Total number of polymer chains: 1
• Total formula weight: 13744.42

Authors

Lytle, B.L.,Peterson, F.C.,Qui, S.H.,Luo, M.,Volkman, B.F.,Markley, J.L.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2004-04-13, release date: 2004-04-27, Last modification date: 2024-05-22)

Primary citation

Lytle, B.L.,Peterson, F.C.,Qiu, S.H.,Luo, M.,Zhao, Q.,Markley, J.L.,Volkman, B.F.
Solution Structure of a Ubiquitin-like Domain from Tubulin-binding Cofactor B.
J.Biol.Chem., 279:46787-46793, 2004

PubMed Abstract: 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.

PubMed: 15364906
DOI: 10.1074/jbc.M409422200

Experimental method

SOLUTION NMR