|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6k4h' size='340' side='right'caption='[[6k4h]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='6k4h' size='340' side='right'caption='[[6k4h]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6k4h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K4H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6k4h]] is a 2 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=6K4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K4H FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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]] 2.55Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3x03|3x03]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PIP4K2B, PIP5K2B ([https://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'>[https://en.wikipedia.org/wiki/1-phosphatidylinositol-5-phosphate_4-kinase 1-phosphatidylinositol-5-phosphate 4-kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.149 2.7.1.149] </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=6k4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k4h OCA], [https://pdbe.org/6k4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k4h RCSB], [https://www.ebi.ac.uk/pdbsum/6k4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k4h ProSAT]</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=6k4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k4h OCA], [https://pdbe.org/6k4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k4h RCSB], [https://www.ebi.ac.uk/pdbsum/6k4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k4h ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PI42B_HUMAN PI42B_HUMAN]] Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate.<ref>PMID:9038203</ref>
| + | [https://www.uniprot.org/uniprot/PI42B_HUMAN PI42B_HUMAN] Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate.<ref>PMID:9038203</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 1-phosphatidylinositol-5-phosphate 4-kinase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Senda, M]] | + | [[Category: Senda M]] |
| - | [[Category: Senda, T]] | + | [[Category: Senda T]] |
| - | [[Category: Takeuchi, K]] | + | [[Category: Takeuchi K]] |
| - | [[Category: Lipid kinase]]
| + | |
| - | [[Category: Phosphoinositide signaling]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PI42B_HUMAN Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate.[1]
Publication Abstract from PubMed
Unlike most kinases, phosphatidylinositol 5-phosphate 4-kinase beta (PI5P4Kbeta) utilizes GTP as a physiological phosphate donor and regulates cell growth under stress (i.e., GTP-dependent stress resilience). However, the genesis and evolution of its GTP responsiveness remain unknown. Here, we reveal that PI5P4Kbeta has acquired GTP preference by generating a short dual-nucleotide-recognizing motif called the guanine efficient association (GEA) motif. Comparison of nucleobase recognition with 660 kinases and 128 G proteins has uncovered that most kinases and PI5P4Kbeta use their main-chain atoms for adenine recognition, while the side-chain atoms are required for guanine recognition. Mutational analysis of the GEA motif revealed that the acquisition of GTP reactivity is accompanied by an extended activity toward inosine triphosphate (ITP) and xanthosine triphosphate (XTP). Along with the evolutionary analysis data that point to strong negative selection of the GEA motif, these results suggest that the GTP responsiveness of PI5P4Kbeta has evolved from a compromised trade-off between activity and specificity, underpinning the development of the GTP-dependent stress resilience.
The GTP responsiveness of PI5P4Kbeta evolved from a compromised trade-off between activity and specificity.,Takeuchi K, Ikeda Y, Senda M, Harada A, Okuwaki K, Fukuzawa K, Nakagawa S, Yu HY, Nagase L, Imai M, Sasaki M, Lo YH, Ito D, Osaka N, Fujii Y, Sasaki AT, Senda T Structure. 2022 Apr 18. pii: S0969-2126(22)00131-9. doi:, 10.1016/j.str.2022.04.004. PMID:35504278[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Castellino AM, Parker GJ, Boronenkov IV, Anderson RA, Chao MV. A novel interaction between the juxtamembrane region of the p55 tumor necrosis factor receptor and phosphatidylinositol-4-phosphate 5-kinase. J Biol Chem. 1997 Feb 28;272(9):5861-70. PMID:9038203
- ↑ Takeuchi K, Ikeda Y, Senda M, Harada A, Okuwaki K, Fukuzawa K, Nakagawa S, Yu HY, Nagase L, Imai M, Sasaki M, Lo YH, Ito D, Osaka N, Fujii Y, Sasaki AT, Senda T. The GTP responsiveness of PI5P4Kbeta evolved from a compromised trade-off between activity and specificity. Structure. 2022 Apr 18. pii: S0969-2126(22)00131-9. doi:, 10.1016/j.str.2022.04.004. PMID:35504278 doi:http://dx.doi.org/10.1016/j.str.2022.04.004
|
