View source for 3udt


==Inositol 1,3,4,5,6-pentakisphosphate 2-kinase from A. thaliana in complex with ADP and IP5.==
<StructureSection load='3udt' size='340' side='right' caption='[[3udt]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3udt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UDT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UDT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5MY:MYO-INOSITOL-(1,3,4,5,6)-PENTAKISPHOSPHATE'>5MY</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3uds|3uds]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At5g42810, IPK1, MJB21.19 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inositol-pentakisphosphate_2-kinase Inositol-pentakisphosphate 2-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.158 2.7.1.158] </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=3udt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3udt OCA], [http://pdbe.org/3udt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3udt RCSB], [http://www.ebi.ac.uk/pdbsum/3udt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3udt ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/IPPK_ARATH IPPK_ARATH]] Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). Phytate is a regulator of intracellular signaling, a highly abundant animal antinutrient, and a phosphate store in plant seeds. Also phosphorylates Ins(1,3,4,6)P4 and Ins(1,4,5,6)P4 to produce Ins(1,2,3,4,6)P5 and Ins(1,2,4,5,6)P5.<ref>PMID:16107538</ref> <ref>PMID:16223361</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Inositol phosphate kinases (IPKs) sequentially phosphorylate inositol phosphates (IPs) on their inositol rings to yield an array of signaling molecules. IPKs must possess the ability to recognize their physiological substrates from among a pool of over 30 cellular IPs that differ in numbers and positions of phosphates. Crystal structures from IPK subfamilies have revealed structural determinants for IP discrimination, which vary considerably between IPKs. However, recent structures of inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IPK1) did not reveal how IPK1 selectively recognizes its physiological substrate, IP5, while excluding others. Here, we report that limited proteolysis has revealed the presence of multiple conformational states in the IPK1 catalytic cycle, with notable protection from protease only in the presence of IP. Further, a 3.1 A crystal structure of IPK1 bound to ADP in the absence of IP revealed decreased order in residues 110-140 within the N-lobe of the kinase compared to structures in which IP is bound. Using this solution and crystallographic data, we propose a model for recognition of IP substrate by IPK1 wherein phosphate groups at the 4-, 5- and 6-positions are recognized initially by the C-lobe with subsequent interaction of the 1-position phosphate by Arg130 that stabilizes this residue and the N-lobe. This model explains how IPK1 can be highly specific for a single IP substrate by linking its interactions with substrate phosphate groups to the stabilization of the N- and C-lobes and kinase activation.

Inositol phosphate-induced stabilization of inositol 1,3,4,5,6-pentakisphosphate 2-kinase and its role in substrate specificity.,Gosein V, Leung TF, Krajden O, Miller GJ Protein Sci. 2012 Feb 23. doi: 10.1002/pro.2049. PMID:22362712<ref>PMID:22362712</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3udt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arath]]
[[Category: Inositol-pentakisphosphate 2-kinase]]
[[Category: Gosein, V]]
[[Category: Krajden, O]]
[[Category: Leung, T F]]
[[Category: Miller, G J]]
[[Category: Atipk1]]
[[Category: Inositol]]
[[Category: Ins5p 2-k]]
[[Category: Ip5 2-k]]
[[Category: Ipk]]
[[Category: Polyphosphate kinase]]
[[Category: Transferase]]