1svw
|
Crystal Structure of YsxC complexed with GMPPNP
OverviewOverview
Genetic analysis has suggested that the product of the Bacillus subtilis, ysxC gene is essential for survival of the microorganism and hence may, represent a target for the development of a novel anti-infective agent., B.subtilis YsxC is a member of the translation factor related class of, GTPases and its crystal structure has been determined in an apo form and, in complex with GDP and GMPPNP/Mg2+. Analysis of these structures has, allowed us to examine the conformational changes that occur during the, process of nucleotide binding and GTP hydrolysis. These structural changes, particularly affect parts of the switch I and switch II region of YsxC, which become ordered and disordered, respectively in the "closed" or "on", GTP-bound state and disordered and ordered, respectively, in the "open" or, "off" GDP-bound conformation. Finally, the binding of the magnesium cation, results in subtle shifts of residues in the G3 region, at the start of, switch II, which serve to optimize the interaction with a key aspartic, acid residue. The structural flexibility observed in YsxC is likely to, contribute to the role of the protein, possibly allowing transduction of, an essential intracellular signal, which may be mediated via interactions, with a conserved patch of surface-exposed, basic residues that lies, adjacent to the GTP-binding site.
About this StructureAbout this Structure
1SVW is a Single protein structure of sequence from Bacillus subtilis with MG and GTP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Analysis of the open and closed conformations of the GTP-binding protein YsxC from Bacillus subtilis., Ruzheinikov SN, Das SK, Sedelnikova SE, Baker PJ, Artymiuk PJ, Garcia-Lara J, Foster SJ, Rice DW, J Mol Biol. 2004 May 28;339(2):265-78. PMID:15136032
Page seeded by OCA on Wed Nov 21 02:46:23 2007