National Center for
3U53: Crystal Structure Of Human Ap4a Hydrolase
Biochem. Biophys. Res. Commun. (2013) 432 p.16-21
ApA hydrolase (asymmetrical diadenosine tetraphosphate hydrolase, EC 220.127.116.11), an enzyme involved in a number of biological processes, is characterized as cleaving the polyphosphate chain at the fourth phosphate from the bound adenosine moiety. This paper presents the crystal structure of wild-type and E58A mutant human ApA hydrolase. Similar to the canonical Nudix fold, human ApA hydrolase shows the common alphabetaalpha-sandwich architecture. Interestingly, two sulfate ions and one diphosphate coordinated with some conserved residues were observed in the active cleft, which affords a better understanding of a possible mode of substrate binding.