4ijx: Difference between revisions
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==Crystal structure of human Ap4A hydrolase E58A mutant complexed with DPO== | ==Crystal structure of human Ap4A hydrolase E58A mutant complexed with DPO== | ||
<StructureSection load='4ijx' size='340' side='right' caption='[[4ijx]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='4ijx' size='340' side='right' caption='[[4ijx]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NUDT2, APAH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NUDT2, APAH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ijx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ijx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ijx RCSB], [http://www.ebi.ac.uk/pdbsum/4ijx PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ijx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ijx OCA], [http://pdbe.org/4ijx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ijx RCSB], [http://www.ebi.ac.uk/pdbsum/4ijx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ijx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ijx" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:53, 4 August 2016
Crystal structure of human Ap4A hydrolase E58A mutant complexed with DPOCrystal structure of human Ap4A hydrolase E58A mutant complexed with DPO
Structural highlights
Function[AP4A_HUMAN] Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis. Publication Abstract from PubMedApA 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 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. Crystal structure of wild-type and mutant human Ap4A hydrolase.,Ge H, Chen X, Yang W, Niu L, Teng M Biochem Biophys Res Commun. 2013 Mar 1;432(1):16-21. doi:, 10.1016/j.bbrc.2013.01.095. Epub 2013 Feb 4. PMID:23384440[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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