4ICK

Crystal structure of human AP4A hydrolase E58A mutant

Summary for 4ICK

• Entry DOI: 10.2210/pdb4ick/pdb
• Related: 3u53
• Descriptor: Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical], GLYCEROL, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: nudix fold, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 35940.07

Authors

Ge, H.,Chen, X. (deposition date: 2012-12-10, release date: 2013-12-11, Last modification date: 2023-11-08)

Primary citation

Ge, H.,Chen, X.,Yang, W.,Niu, L.,Teng, M.
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 (2.1 Å)