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Crystal structure of wild-type and mutant human Ap4A hydrolase.

Abstract：

:Ap4A hydrolase (asymmetrical diadenosine tetraphosphate hydrolase, EC 3.6.1.17), 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 Ap4A hydrolase. Similar to the canonical Nudix fold, human Ap4A hydrolase shows the common αβα-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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Ge H,Chen X,Yang W,Niu L,Teng M

doi

10.1016/j.bbrc.2013.01.095

subject

Has Abstract

pub_date

2013-03-01 00:00:00

pages

16-21

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(13)00185-X

journal_volume

432

pub_type

杂志文章

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