3c12
Crystal Structure of FlgD from Xanthomonas campestris: Insights into the Hook Capping Essential for Flagellar AssemblyCrystal Structure of FlgD from Xanthomonas campestris: Insights into the Hook Capping Essential for Flagellar Assembly
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. References
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