1ktg

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(New page: 200px<br /><applet load="1ktg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ktg, resolution 1.80&Aring;" /> '''Crystal Structure of...)
Current revision (09:04, 16 August 2023) (edit) (undo)
 
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[[Image:1ktg.gif|left|200px]]<br /><applet load="1ktg" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ktg, resolution 1.80&Aring;" />
 
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'''Crystal Structure of a C. elegans Ap4A Hydrolase Binary Complex'''<br />
 
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==Overview==
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==Crystal Structure of a C. elegans Ap4A Hydrolase Binary Complex==
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The crystal structure of C. elegans Ap(4)A hydrolase has been determined, for the free enzyme and a binary complex at 2.0 A and 1.8 A, respectively., Ap(4)A hydrolase has a key role in regulating the intracellular Ap(4)A, levels and hence potentially the cellular response to metabolic stress, and/or differentiation and apoptosis via the Ap(3)A/Ap(4)A ratio. The, structures reveal that the enzyme has the mixed alpha/beta fold of the, Nudix family and also show how the enzyme binds and locates its substrate, with respect to the catalytic machinery of the Nudix motif. These results, suggest how the enzyme can catalyze the hydrolysis of a range of related, dinucleoside tetraphosphate, but not triphosphate, compounds through, precise orientation of key elements of the substrate.
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<StructureSection load='1ktg' size='340' side='right'caption='[[1ktg]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ktg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KTG FirstGlance]. <br>
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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]] 1.8&#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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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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=1ktg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ktg OCA], [https://pdbe.org/1ktg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ktg RCSB], [https://www.ebi.ac.uk/pdbsum/1ktg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ktg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AP4A_CAEEL AP4A_CAEEL] Asymmetrically hydrolyzes Ap4A to yield AMP and ATP.<ref>PMID:11738085</ref>
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== Evolutionary Conservation ==
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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/kt/1ktg_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=1ktg 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 ==
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The crystal structure of C. elegans Ap(4)A hydrolase has been determined for the free enzyme and a binary complex at 2.0 A and 1.8 A, respectively. Ap(4)A hydrolase has a key role in regulating the intracellular Ap(4)A levels and hence potentially the cellular response to metabolic stress and/or differentiation and apoptosis via the Ap(3)A/Ap(4)A ratio. The structures reveal that the enzyme has the mixed alpha/beta fold of the Nudix family and also show how the enzyme binds and locates its substrate with respect to the catalytic machinery of the Nudix motif. These results suggest how the enzyme can catalyze the hydrolysis of a range of related dinucleoside tetraphosphate, but not triphosphate, compounds through precise orientation of key elements of the substrate.
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==About this Structure==
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The crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms.,Bailey S, Sedelnikova SE, Blackburn GM, Abdelghany HM, Baker PJ, McLennan AG, Rafferty JB Structure. 2002 Apr;10(4):589-600. PMID:11937063<ref>PMID:11937063</ref>
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1KTG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] with PO4, OH, MG and AMP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KTG 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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The crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms., Bailey S, Sedelnikova SE, Blackburn GM, Abdelghany HM, Baker PJ, McLennan AG, Rafferty JB, Structure. 2002 Apr;10(4):589-600. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11937063 11937063]
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</div>
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[[Category: Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)]]
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<div class="pdbe-citations 1ktg" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Abdelghany, H.M.]]
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[[Category: Abdelghany HM]]
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[[Category: Bailey, S.]]
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[[Category: Bailey S]]
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[[Category: Baker, P.J.]]
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[[Category: Baker PJ]]
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[[Category: Blackburn, G.M.]]
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[[Category: Blackburn GM]]
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[[Category: McLennan, A.G.]]
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[[Category: McLennan AG]]
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[[Category: Rafferty, J.B.]]
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[[Category: Rafferty JB]]
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[[Category: Sedelnikova, S.E.]]
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[[Category: Sedelnikova SE]]
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[[Category: AMP]]
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[[Category: MG]]
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[[Category: OH]]
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[[Category: PO4]]
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[[Category: amp]]
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[[Category: magnesium cluster]]
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[[Category: nudix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:51:16 2007''
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Current revision

Crystal Structure of a C. elegans Ap4A Hydrolase Binary Complex

PDB ID 1ktg

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