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4c6a

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<StructureSection load='4c6a' size='340' side='right'caption='[[4c6a]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
<StructureSection load='4c6a' size='340' side='right'caption='[[4c6a]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4c6a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dicdi Dicdi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C6A FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4c6a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C6A FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] </span></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=4c6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6a OCA], [https://pdbe.org/4c6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c6a RCSB], [https://www.ebi.ac.uk/pdbsum/4c6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6a ProSAT]</span></td></tr>
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<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=4c6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6a OCA], [http://pdbe.org/4c6a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c6a RCSB], [http://www.ebi.ac.uk/pdbsum/4c6a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6a ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[[https://www.uniprot.org/uniprot/NDKC_DICDI NDKC_DICDI]]
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The acyclic nucleosides thiophosphonates (9-[2-(thiophosphonomethoxy)ethyl]adenine (S-PMEA) and (R)-9-[2-(thiophosphonomethoxy)propyl]adenine (S-PMPA), exhibit antiviral activity against HIV-1, -2 and HBV. Their diphosphate forms S-PMEApp and S-PMPApp, synthesized as stereoisomeric mixture, are potent inhibitors of wild-type (WT) HIV-1 RT. Understanding HIV-1 RT stereoselectivity, however, awaits resolution of the diphosphate forms into defined stereoisomers. To this aim, thiophosphonate monophosphates S-PMEAp and S-PMPAp were synthesized and used in a stereocontrolled enzyme-catalyzed phosphoryl transfer reaction involving either nucleoside diphosphate kinase (NDPK) or creatine kinase (CK) to obtain thiophosphonate diphosphates as separated isomers. We then quantified substrate preference of recombinant WT HIV-1 RT toward pure stereoisomers using in vitro steady-state kinetic analyses. The crystal structure of a complex between Dictyostelium NDPK and S-PMPApp at 2.32A allowed to determine the absolute configuration at the alpha-phosphorus atom in relation to the stereo-preference of studied enzymes. The RP isomer of S-PMPApp and S-PMEApp are the preferred substrate over SP for both NDPK and HIV-1 RT.
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Enzymatic synthesis of acyclic nucleoside thiophosphonate diphosphates: Effect of the alpha-phosphorus configuration on HIV-1 RT activity.,Priet S, Roux L, Saez-Ayala M, Ferron F, Canard B, Alvarez K Antiviral Res. 2015 Mar 9;117:122-131. doi: 10.1016/j.antiviral.2015.03.003. PMID:25766862<ref>PMID:25766862</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4c6a" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Nucleoside diphosphate kinase|Nucleoside diphosphate kinase]]
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*[[Nucleoside diphosphate kinase 3D structures|Nucleoside diphosphate kinase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Dicdi]]
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[[Category: Dictyostelium discoideum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Nucleoside-diphosphate kinase]]
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[[Category: Alvarez K]]
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[[Category: Alvarez, K]]
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[[Category: Canard B]]
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[[Category: Canard, B]]
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[[Category: Ferron F]]
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[[Category: Ferron, F]]
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[[Category: Priet S]]
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[[Category: Priet, S]]
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[[Category: Verron M]]
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[[Category: Verron, M]]
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[[Category: Phosphotransferase]]
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[[Category: Transferase]]
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Revision as of 17:28, 7 September 2022

High Resolution Structure of the Nucleoside diphosphate kinase

PDB ID 4c6a

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