Crystal structure of wild-type and mutant human Ap4A hydrolase.
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ABSTRACT:
SUBMITTER: Ge H
PROVIDER: S-EPMC7092880 | biostudies-literature | 2013 Mar
REPOSITORIES: biostudies-literature
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Crystal structure of wild-type and mutant human Ap4A hydrolase.
Ge Honghua H Chen Xiaofang X Yang Weili W Niu Liwen L Teng Maikun M
Biochemical and biophysical research communications 20130204 1
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 coordi ...[more]
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