4ick: Difference between revisions

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~~{{STRUCTURE_4ick| PDB=4ick | SCENE= }}~~

==Crystal structure of human AP4A hydrolase E58A mutant==

===Crystal structure of human AP4A hydrolase E58A mutant===

~~{{ABSTRACT_PUBMED_23384440}}~~

== Structural highlights ==

<table><tr><td colspan='2'>[[4ick]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ICK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ICK FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3u53|3u53]]</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='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=4ick FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ick OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ick RCSB], [http://www.ebi.ac.uk/pdbsum/4ick PDBsum]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

ApA 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.

~~==Function==~~

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<ref>PMID:23384440</ref>

~~[[http~~:/~~/www~~.~~uniprot~~.~~org/uniprot/AP4A_HUMAN AP4A_HUMAN]] Asymmetrically hydrolyzes Ap4A to yield AMP and ATP~~. ~~Plays a major role in maintaining homeostasis~~.

~~==About this Structure==~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

~~[[4ick]] is~~ a ~~2 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4ICK OCA].~~

</div>

== References ==

==~~Reference~~==

~~<ref group="xtra">PMID:023384440</ref>~~<references ~~group="xtra"~~/><~~references~~/>

__TOC__

[[Category: Chen, X.]]

</StructureSection>

[[Category: Ge, H.]]

[[Category: Human]]

[[Category: Chen, X]]

[[Category: Ge, H]]

[[Category: Hydrolase]]

[[Category: Nudix fold]]

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@@ Line 1: / Line 1: @@
-{{STRUCTURE_4ick|  PDB=4ick  |  SCENE=  }}
+==Crystal structure of human AP4A hydrolase E58A mutant==
-===Crystal structure of human AP4A hydrolase E58A mutant===
+<StructureSection load='4ick' size='340' side='right' caption='[[4ick]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-{{ABSTRACT_PUBMED_23384440}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4ick]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ICK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ICK FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3u53|3u53]]</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='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=4ick FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ick OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ick RCSB], [http://www.ebi.ac.uk/pdbsum/4ick PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+ApA 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.
-==Function==
+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<ref>PMID:23384440</ref>
-[[http://www.uniprot.org/uniprot/AP4A_HUMAN AP4A_HUMAN]] Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[4ick]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ICK OCA].
+</div>
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:023384440</ref><references group="xtra"/><references/>
+__TOC__
-[[Category: Chen, X.]]
+</StructureSection>
-[[Category: Ge, H.]]
+[[Category: Human]]
+[[Category: Chen, X]]
+[[Category: Ge, H]]
 [[Category: Hydrolase]]
 [[Category: Nudix fold]]