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| | <StructureSection load='4o4c' size='340' side='right'caption='[[4o4c]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='4o4c' size='340' side='right'caption='[[4o4c]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4o4c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Entamoeba_histolytica_hm-1:imss-a Entamoeba histolytica hm-1:imss-a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O4C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O4C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4o4c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica_HM-1:IMSS-A Entamoeba histolytica HM-1:IMSS-A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O4C FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o4b|4o4b]], [[4o4d|4o4d]], [[4o4e|4o4e]], [[4o4f|4o4f]]</td></tr> | + | </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=4o4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o4c OCA], [https://pdbe.org/4o4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o4c RCSB], [https://www.ebi.ac.uk/pdbsum/4o4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o4c ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHI7A_103520 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=885318 Entamoeba histolytica HM-1:IMSS-A])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inositol-hexakisphosphate_kinase Inositol-hexakisphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.21 2.7.4.21] </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=4o4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o4c OCA], [http://pdbe.org/4o4c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o4c RCSB], [http://www.ebi.ac.uk/pdbsum/4o4c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o4c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/N9UNA8_ENTH1 N9UNA8_ENTH1] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Entamoeba histolytica hm-1:imss-a]] | + | [[Category: Entamoeba histolytica HM-1:IMSS-A]] |
| - | [[Category: Inositol-hexakisphosphate kinase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Shears, S B]] | + | [[Category: Shears SB]] |
| - | [[Category: Wang, H]] | + | [[Category: Wang H]] |
| - | [[Category: Inositol phosphate]]
| + | |
| - | [[Category: Pdkg kinase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
N9UNA8_ENTH1
Publication Abstract from PubMed
Inositol trisphosphate kinases (IP3Ks) and inositol hexakisphosphate kinases (IP6Ks) each regulate specialized signalling activities by phosphorylating either InsP3 or InsP6 respectively. The molecular basis for these different kinase activities can be illuminated by a structural description of IP6K. Here we describe the crystal structure of an Entamoeba histolytica hybrid IP6K/IP3K, an enzymatic parallel to a 'living fossil'. Through molecular modelling and mutagenesis, we extrapolated our findings to human IP6K2, which retains vestigial IP3K activity. Two structural elements, an alpha-helical pair and a rare, two-turn 310 helix, together forge a substrate-binding pocket with an open clamshell geometry. InsP6 forms substantial contacts with both structural elements. Relative to InsP6, enzyme-bound InsP3 rotates 55 degrees closer to the alpha-helices, which provide most of the protein's interactions with InsP3. These data reveal the molecular determinants of IP6K activity, and suggest an unusual evolutionary trajectory for a primordial kinase that could have favored efficient bifunctionality, before propagation of separate IP3Ks and IP6Ks.
IP6K structure and the molecular determinants of catalytic specificity in an inositol phosphate kinase family.,Wang H, DeRose EF, London RE, Shears SB Nat Commun. 2014 Jun 24;5:4178. doi: 10.1038/ncomms5178. PMID:24956979[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang H, DeRose EF, London RE, Shears SB. IP6K structure and the molecular determinants of catalytic specificity in an inositol phosphate kinase family. Nat Commun. 2014 Jun 24;5:4178. doi: 10.1038/ncomms5178. PMID:24956979 doi:http://dx.doi.org/10.1038/ncomms5178
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