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| | <StructureSection load='6wg5' size='340' side='right'caption='[[6wg5]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='6wg5' size='340' side='right'caption='[[6wg5]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6wg5]] is a 1 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=6WG5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WG5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6wg5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WG5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ENTPD4, KIAA0392, LALP70, LYSAL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside_diphosphate_phosphatase Nucleoside diphosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.6 3.6.1.6] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6wg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wg5 OCA], [https://pdbe.org/6wg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wg5 RCSB], [https://www.ebi.ac.uk/pdbsum/6wg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wg5 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6wg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wg5 OCA], [http://pdbe.org/6wg5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wg5 RCSB], [http://www.ebi.ac.uk/pdbsum/6wg5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wg5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ENTP4_HUMAN ENTP4_HUMAN]] Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent. The order of activity with different substrates is UDP >> GDP = CDP = TDP, AMP, ADP, ATP and UMP are not substrates. Preferred substrates for isoform 2 are CTP, UDP, CDP, GTP and GDP, while isoform 1 utilizes UTP and TTP. | + | [https://www.uniprot.org/uniprot/ENTP4_HUMAN ENTP4_HUMAN] Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent. The order of activity with different substrates is UDP >> GDP = CDP = TDP, AMP, ADP, ATP and UMP are not substrates. Preferred substrates for isoform 2 are CTP, UDP, CDP, GTP and GDP, while isoform 1 utilizes UTP and TTP. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6wg5" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6wg5" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ectonucleoside triphosphate diphosphohydrolase|Ectonucleoside triphosphate diphosphohydrolase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nucleoside diphosphate phosphatase]]
| + | [[Category: Gorelik A]] |
| - | [[Category: Gorelik, A]] | + | [[Category: Illes K]] |
| - | [[Category: Illes, K]] | + | [[Category: Labriola JM]] |
| - | [[Category: Labriola, J M]] | + | [[Category: Nagar B]] |
| - | [[Category: Nagar, B]] | + | |
| - | [[Category: Askha superfamily]]
| + | |
| - | [[Category: Glycosylation]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nucleotide metabolism]]
| + | |
| Structural highlights
Function
ENTP4_HUMAN Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent. The order of activity with different substrates is UDP >> GDP = CDP = TDP, AMP, ADP, ATP and UMP are not substrates. Preferred substrates for isoform 2 are CTP, UDP, CDP, GTP and GDP, while isoform 1 utilizes UTP and TTP.
Publication Abstract from PubMed
The ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are a family of enzymes found on the cell surface and in the lumen of certain organelles that are major regulators of purinergic signaling. Their intracellular roles, however, have not been clearly defined. NTPDase4 (UDPase, ENTPD4) is a Golgi protein potentially involved in nucleotide recycling as part of protein glycosylation, and is also found in lysosomes, where its purpose is unknown. To further our understanding of NTPDase4 function, we determined its crystal structure. The enzyme adopts a wide open, inactive conformation. Differences in the nucleotide-binding site relative to its homologs could account for its substrate selectivity. The putative membrane-interacting loop of cell-surface NTPDases is drastically altered in NTPDase4, potentially affecting its inter-domain dynamics at the Golgi membrane. This article is protected by copyright. All rights reserved.
Crystal structure of the nucleotide-metabolizing enzyme NTPDase4.,Gorelik A, Labriola JM, Illes K, Nagar B Protein Sci. 2020 Aug 6. doi: 10.1002/pro.3926. PMID:32767432[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gorelik A, Labriola JM, Illes K, Nagar B. Crystal structure of the nucleotide-metabolizing enzyme NTPDase4. Protein Sci. 2020 Aug 6. doi: 10.1002/pro.3926. PMID:32767432 doi:http://dx.doi.org/10.1002/pro.3926
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