3MXZ

Crystal Structure of tubulin folding cofactor A from Arabidopsis thaliana

Summary for 3MXZ

• Entry DOI: 10.2210/pdb3mxz/pdb
• Descriptor: Tubulin-specific chaperone A, NITRATE ION (3 entities in total)
• Functional Keywords: helix bundle, chaperone
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 1
• Total formula weight: 13252.80

Authors

Lu, L.,Nan, J.,Mi, W.,Su, X.D.,Li, Y. (deposition date: 2010-05-08, release date: 2010-09-01, Last modification date: 2023-11-01)

Primary citation

Lu, L.,Nan, J.,Mi, W.,Li, L.F.,Wei, C.H.,Su, X.D.,Li, Y.
Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its beta-tubulin binding characterization
Febs Lett., 584:3533-3539, 2010

PubMed Abstract: Microtubules are composed of polymerized alpha/beta-tubulin heterodimers. Biogenesis of assembly-competent tubulin dimers is a complex multistep process that requires sequential actions of distinct molecular chaperones and cofactors. Tubulin folding cofactor A (TFCA), which captures beta-tubulin during the folding pathway, has been identified in many organisms. Here, we report the crystal structure of Arabidopsis thaliana TFC A (KIESEL, KIS), which forms a monomeric three-helix bundle. The functional binding analysis demonstrated that KIS interacts with beta-tubulin in plant. Furthermore, mutagenesis studies indicated that the alpha-helical regions of KIS participate in beta-tubulin binding. Unlike the budding yeast TFC A, the two loop regions of KIS are not required for this interaction suggesting a distinct binding mechanism of TFC A to beta-tubulin in plants.

PubMed: 20638386
DOI: 10.1016/j.febslet.2010.07.017

Experimental method

X-RAY DIFFRACTION (1.599 Å)