3C12

Crystal Structure of FlgD from Xanthomonas campestris: Insights into the Hook Capping Essential for Flagellar Assembly

Summary for 3C12

• Entry DOI: 10.2210/pdb3c12/pdb
• Descriptor: Flagellar protein (2 entities in total)
• Functional Keywords: flgd, hook capping, xanthomonas campestris, ig-like domain, fn-iii domain, tudor-like domain, flagellar biogenesis, flagellum, biosynthetic protein
• Biological source: Xanthomonas campestris pv. campestris
• Total number of polymer chains: 1
• Total formula weight: 13738.25

Authors

Kuo, W.-T.,Chin, K.-H.,Lo, W.-T.,Chou, S.-H. (deposition date: 2008-01-22, release date: 2008-12-09, Last modification date: 2024-03-13)

Primary citation

Kuo, W.-T.,Chin, K.-H.,Lo, W.-T.,Wang, A.H.-J.,Chou, S.-H.
Crystal structure of the C-terminal domain of a flagellar hook-capping protein from Xanthomonas campestris
J.Mol.Biol., 381:189-199, 2008

PubMed 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 A 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.

PubMed: 18599076
DOI: 10.1016/j.jmb.2008.05.083

Experimental method

X-RAY DIFFRACTION (2.51 Å)