3U53

Crystal structure of human Ap4A hydrolase

Summary for 3U53

• Entry DOI: 10.2210/pdb3u53/pdb
• Descriptor: Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical], SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 4
• Total formula weight: 73414.70

Authors

Ge, H.H.,Teng, M.K. (deposition date: 2011-10-10, release date: 2012-10-10, Last modification date: 2023-11-01)

Primary citation

Ge, H.H.,Chen, X.F.,Yang, W.L.,Niu, L.W.,Teng, M.K.
Crystal structure of wild-type and mutant human Ap4A hydrolase
Biochem.Biophys.Res.Commun., 432:16-21, 2013

PubMed 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.

PubMed: 23384440
DOI: 10.1016/j.bbrc.2013.01.095

Experimental method

X-RAY DIFFRACTION (2.705 Å)