2ftk
From Proteopedia
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berylloflouride Spo0F complex with Spo0B
Overview
A number of regulatory circuits in biological systems function through the, exchange of phosphoryl groups from one protein to another. Spo0F and Spo0B, are components of a phosphorelay that control sporulation in the bacterium, Bacillus subtilis through the exchange of a phosphoryl group. Using, beryllofluoride as a mimic for phosphorylation, we trapped the interaction, of the phosphorylated Spo0F with Spo0B in the crystal lattice. The, transition state of phosphoryl transfer continues to be a highly debated, issue, as to whether it is associative or dissociative in nature. The, geometry of Spo0F binding to Spo0B favors an associative mechanism for, phosphoryl transfer. In order to visualize the autophosphorylation of the, histidine kinase, KinA, and the subsequent phosphoryl transfer to Spo0F, we generated in silico models representing these reaction steps.
About this Structure
2FTK is a Protein complex structure of sequences from Bacillus subtilis with MG as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition state., Varughese KI, Tsigelny I, Zhao H, J Bacteriol. 2006 Jul;188(13):4970-7. PMID:16788205
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