Histidine 114 Is Critical for XXXX Hydrolysis by the Universally Conserved ATPase YchF.

@entity3007 @entity526 @entity4334 @entity3689 @entity855
GTPases perform a wide range of functions, ranging from protein synthesis to cell signaling. Of all known GTPases, only eight are conserved across all three domains of life. YchF is one of these eight universally conserved GTPases; however, its cellular function and enzymatic properties are poorly understood. YchF differs from the classical GTPases in that it has a higher affinity for @entity855 than for @entity3007 and is a functional ATPase. As a hydrophobic @entity3689 -substituted ATPase, YchF does not possess the canonical catalytic Gln required for @entity4334 hydrolysis. To elucidate the catalytic mechanism of @entity855 hydrolysis by YchF, we have taken a two-pronged approach combining classical biochemical and in silico techniques. The use of molecular dynamics simulations allowed us to complement our biochemical findings with information about the structural dynamics of YchF. We have thereby identified the highly conserved His-114 as critical for the ATPase activity of YchF from @entity526 . His-114 is located in a flexible loop of the G-domain, which undergoes @entity4334 -dependent conformational changes. The use of a catalytic His is also observed in the hydrophobic @entity3689 -substituted GTPase RbgA and is an identifier of the translational GTPase family.
