P-loop containing nucleoside triphosphate hydrolase QuickView

Description:: The P-loop NTPase fold is the most prevalent domain of the several distinctnucleotide-binding protein folds.The most common reaction catalysed by enzymes of the P-loop NTPase fold is the hydrolysis of the beta-gamma phosphate bond of a bound nucleoside triphosphate (NTP). The energy from NTP hydrolysis is typically utilised to induce conformational changes in other molecules, which constitutes the basis of the biological functions of most P-loop NTPases. P-loop NTPases show substantial substrate preference for either ATP or GTP. P-loop NTPases are characterised by two conserved sequence signatures, theWalker A motif (the P-loop proper) and Walker B motifs which bind, respectively, the beta and gamma phosphate moieties of the bound NTP, and a Mg2+ cation.P-loop ATPase domains belong to one of the two major divisions. The kinase-GTPase (KG) division includes the kinases and GTPases, and the ASCE division, characterised by an additional strand in the core sheet, which is locatedbetween the P-loop strand and the Walker B strand. Most members of the ASCE division utilise ATP and members of this group include AAA+, ABC, PilT, HerA-FtsK, superfamily 1/2 (SF1/2) helicases, and the RecA/ATP-synthase superfamilies of ATPases, etc.