Publication Abstract from PubMed
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.
Crystal structure of the C-terminal domain of a flagellar hook-capping protein from Xanthomonas campestris.,Kuo WT, Chin KH, Lo WT, Wang AH, Chou SH J Mol Biol. 2008 Aug 1;381(1):189-99. Epub 2008 Jun 7. PMID:18599076[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
