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  • Lu, Lu (author)

Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana and its beta-tubulin binding characterization

  • Article/chapterEnglish2010

Publisher, publication year, extent ...

  • 2010-07-16
  • Wiley,2010
  • 7 s.

Numbers

  • LIBRIS-ID:oai:lup.lub.lu.se:88c0406d-5a12-4137-a2af-387abdfc8bfa
  • https://lup.lub.lu.se/record/88c0406d-5a12-4137-a2af-387abdfc8bfaURI
  • https://doi.org/10.1016/j.febslet.2010.07.017DOI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

Classification

  • Subject category:art swepub-publicationtype
  • Subject category:ref swepub-contenttype

Notes

  • 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.

Subject headings and genre

  • 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

Added entries (persons, corporate bodies, meetings, titles ...)

  • Nan, JieLund University,Lunds universitet,MAX IV-laboratoriet,MAX IV Laboratory,Peking University(Swepub:lu)maxl-jna (author)
  • Mi, Wei (author)
  • Li, Lan-Fen (author)
  • Wei, Chun-Hong (author)
  • Su, Xiao-DongLund 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(Swepub:lu)mbfys-xs (author)
  • Li, Yi (author)
  • Lunds universitetMAX IV-laboratoriet (creator_code:org_t)

Related titles

  • In:FEBS Letters: Wiley584:16, s. 9-35331873-34680014-5793

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