Crystal Structure of the C-Terminal Domain of a Flagellar Hook-Capping Protein from Xanthomonas campestris

Wei Ting Kuo, Ko Hsin Chin, Wen Ting Lo, Andrew H.J. Wang, Shan Ho Chou

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

Abstract

The crystal structure of the C-terminal domain of a hook-capping protein FlgD from the plant pathogen Xanthomonas campestris (Xc) has been determined to a resolution of ca 2.5 Å using X-ray crystallography. The monomer of whole FlgD comprises 221 amino acids with a molecular mass of 22.7 kDa, but the flexible N-terminus is cleaved for up to 75 residues during crystallization. The final structure of the C-terminal domain reveals a novel hybrid comprising a tudor-like domain interdigitated with a fibronectin type III domain. The C-terminal domain of XcFlgD forms three types of dimers in the crystal. In agreement with this, analytical ultracentrifugation and gel filtration experiments reveal that they form a stable dimer in solution. From these results, we propose that the Xc flagellar hook cap protein FlgD comprises two individual domains, a flexible N-terminal domain that cannot be detected in the current study and a stable C-terminal domain that forms a stable dimer.

Original languageEnglish
Pages (from-to)189-199
Number of pages11
JournalJournal of Molecular Biology
Volume381
Issue number1
DOIs
Publication statusPublished - Aug 1 2008
Externally publishedYes

Keywords

  • FlgD
  • hook capping
  • Ig-like domain
  • Tudor-like domain
  • Xanthomonas campestris

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology

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