Search: onr:"swepub:oai:lup.lub.lu.se:88c0406d-5a12-4137-a2af-387abdfc8bfa" >
Crystal structure o...
Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its beta-tubulin binding characterization
-
Lu, Lu (author)
-
- Nan, Jie (author)
- Lund University,Lunds universitet,MAX IV-laboratoriet,MAX IV Laboratory,Peking University
-
Mi, Wei (author)
-
show more...
-
Li, Lan-Fen (author)
-
Wei, Chun-Hong (author)
-
- Su, Xiao-Dong (author)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
-
Li, Yi (author)
-
show less...
-
(creator_code:org_t)
- 2010-07-16
- 2010
- English 7 s.
-
In: FEBS Letters. - : Wiley. - 1873-3468 .- 0014-5793. ; 584:16, s. 9-3533
- Related links:
-
http://dx.doi.org/10...
-
show more...
-
https://lup.lub.lu.s...
-
https://doi.org/10.1...
-
show less...
Abstract
Subject headings
Close
- 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.
Keyword
- Amino Acid Sequence
- Arabidopsis
- Arabidopsis Proteins
- Crystallography, X-Ray
- Genes, Plant
- Genetic Complementation Test
- Microtubule-Associated Proteins
- Models, Molecular
- Molecular Chaperones
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Plants, Genetically Modified
- Protein Binding
- Protein Folding
- Protein Interaction Domains and Motifs
- Protein Structure, Secondary
- Recombinant Proteins
- Sequence Homology, Amino Acid
- Tubulin
Publication and Content Type
- art (subject category)
- ref (subject category)
Find in a library
To the university's database