Sessions 4 4 binds.Neither the extended conformation of the donor analogue nor the induced fit it causes in the protein have been observed before in an rGT.Comparison with the previously determined binary and ternary complexes of Kre2p/Mnt1p with its GDP donor product reveals that the GDP moiety of the GDP-2F-Man is bound in a similar manner.However, its β-phosphate group is in a different position, consistent with the attached 2-fluoro-mannose moiety being buried in the pocket.A triad of charged residues, E247, R245 and D361, is involved in the formation of the pocket due to conformational changes of the R245 and D361 side chains.The carboxylate group of E247 is 3.3 Å from the reactive centre, the β-face of the C1 group of mannose, suggesting its involvement in the reaction mechanism.When the donor analogue is bound, R245 no longer interacts with E247, making E247 even more catalytically relevant.Two triad residues have been shown to be essential for catalysis by sitedirected mutagenesis, and all are structurally conserved in most rGT structures, which suggests that the proposed catalytic mechanism relying on the concerted action of charged triad residues could potentially be a common mechanism for most rGTs.
The structure of the title compound, [RuCl 2 (C 7 H 10 N 2 ) 2 (C 2 H 6 OS) 2 ], has monoclinic ( P 2 1 / n ) symmetry. The Ru—N distances of the coordination compound are influenced by the trans chloride or dimethylsulfoxide-κ S ligands. The molecular structure exhibits disorder for two of the terminal methyl groups of a dimethyl sulfoxide ligand.
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