1z2p

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[[Image:1z2p.gif|left|200px]]
 
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==Inositol 1,3,4-trisphosphate 5/6-Kinase in complex with Mg2+/AMP-PCP/Ins(1,3,4)P3==
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The line below this paragraph, containing "STRUCTURE_1z2p", creates the "Structure Box" on the page.
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<StructureSection load='1z2p' size='340' side='right'caption='[[1z2p]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1z2p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica_HM-1:IMSS Entamoeba histolytica HM-1:IMSS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z2P FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.22&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=I3S:(1S,3S,4S)-1,3,4-TRIPHOSPHO-MYO-INOSITOL'>I3S</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_1z2p| PDB=1z2p | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z2p OCA], [https://pdbe.org/1z2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z2p RCSB], [https://www.ebi.ac.uk/pdbsum/1z2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z2p ProSAT]</span></td></tr>
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</table>
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'''Inositol 1,3,4-trisphosphate 5/6-Kinase in complex with Mg2+/AMP-PCP/Ins(1,3,4)P3'''
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== Function ==
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[https://www.uniprot.org/uniprot/ITPK1_ENTH1 ITPK1_ENTH1] Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. Phosphorylates Ins(3,4,5,6)P4 at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5 is not. Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate (InsP6) pathway. May also act as an isomerase that interconverts the inositol tetrakisphosphate isomers Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the presence of ADP and magnesium.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z2/1z2p_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1z2p ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Inositol hexakisphosphate and other inositol high polyphosphates have diverse and critical roles in eukaryotic regulatory pathways. Inositol 1,3,4-trisphosphate 5/6-kinase catalyzes the rate-limiting step in inositol high polyphosphate synthesis in animals. This multifunctional enzyme also has inositol 3,4,5,6-tetrakisphosphate 1-kinase and other activities. The structure of an archetypal family member, from Entamoeba histolytica, has been determined to 1.2 A resolution in binary and ternary complexes with nucleotide, substrate, and product. The structure reveals an ATP-grasp fold. The inositol ring faces ATP edge-on such that the 5- and 6-hydroxyl groups are nearly equidistant from the ATP gamma-phosphate in catalytically productive phosphoacceptor positions and explains the unusual dual site specificity of this kinase. Inositol tris- and tetrakisphosphates interact via three phosphate binding subsites and one solvent-exposed site that could in principle be occupied by 18 different substrates, explaining the mechanisms for the multiple specificities and catalytic activities of this enzyme.
Inositol hexakisphosphate and other inositol high polyphosphates have diverse and critical roles in eukaryotic regulatory pathways. Inositol 1,3,4-trisphosphate 5/6-kinase catalyzes the rate-limiting step in inositol high polyphosphate synthesis in animals. This multifunctional enzyme also has inositol 3,4,5,6-tetrakisphosphate 1-kinase and other activities. The structure of an archetypal family member, from Entamoeba histolytica, has been determined to 1.2 A resolution in binary and ternary complexes with nucleotide, substrate, and product. The structure reveals an ATP-grasp fold. The inositol ring faces ATP edge-on such that the 5- and 6-hydroxyl groups are nearly equidistant from the ATP gamma-phosphate in catalytically productive phosphoacceptor positions and explains the unusual dual site specificity of this kinase. Inositol tris- and tetrakisphosphates interact via three phosphate binding subsites and one solvent-exposed site that could in principle be occupied by 18 different substrates, explaining the mechanisms for the multiple specificities and catalytic activities of this enzyme.
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==About this Structure==
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Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase.,Miller GJ, Wilson MP, Majerus PW, Hurley JH Mol Cell. 2005 Apr 15;18(2):201-12. PMID:15837423<ref>PMID:15837423</ref>
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1Z2P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z2P OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase., Miller GJ, Wilson MP, Majerus PW, Hurley JH, Mol Cell. 2005 Apr 15;18(2):201-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15837423 15837423]
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</div>
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[[Category: Eukaryota]]
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<div class="pdbe-citations 1z2p" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Hurley, J H.]]
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<references/>
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[[Category: Majerus, P W.]]
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__TOC__
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[[Category: Miller, G J.]]
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</StructureSection>
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[[Category: Wilson, M P.]]
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[[Category: Entamoeba histolytica HM-1:IMSS]]
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[[Category: Atp-grasp]]
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[[Category: Large Structures]]
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[[Category: Inositol phosphate kinase]]
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[[Category: Hurley JH]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:06:50 2008''
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[[Category: Majerus PW]]
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[[Category: Miller GJ]]
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[[Category: Wilson MP]]

Current revision

Inositol 1,3,4-trisphosphate 5/6-Kinase in complex with Mg2+/AMP-PCP/Ins(1,3,4)P3

PDB ID 1z2p

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