View source for 7em2


==Crystal structure of the PI5P4Kbeta-XTP complex==
<StructureSection load='7em2' size='340' side='right'caption='[[7em2]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7em2]] 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=7EM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EM2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CZC:[(2~{R},3~{S},4~{R},5~{R})-5-[2,6-bis(oxidanylidene)-3~{H}-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl+phosphono+hydrogen+phosphate'>CZC</scene>, <scene name='pdbligand=CZF:[[(2~{R},3~{S},4~{R},5~{R})-5-[2,6-bis(oxidanylidene)-3~{H}-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]+phosphono+hydrogen+phosphate'>CZF</scene></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=7em2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7em2 OCA], [https://pdbe.org/7em2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7em2 RCSB], [https://www.ebi.ac.uk/pdbsum/7em2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7em2 ProSAT]</span></td></tr>
</table>
== Function ==
[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;">
== 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<ref>PMID:35504278</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7em2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Senda M]]
[[Category: Senda T]]