6jbc

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<StructureSection load='6jbc' size='340' side='right'caption='[[6jbc]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='6jbc' size='340' side='right'caption='[[6jbc]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6jbc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JBC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6jbc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_kodakaraensis_(strain_kod1) Pyrococcus kodakaraensis (strain kod1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JBC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JBC 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TK2141 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pantoate_kinase Pantoate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.169 2.7.1.169] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pantoate_kinase Pantoate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.169 2.7.1.169] </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=6jbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jbc OCA], [http://pdbe.org/6jbc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jbc RCSB], [http://www.ebi.ac.uk/pdbsum/6jbc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jbc 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://proteopedia.org/fgij/fg.htm?mol=6jbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jbc OCA], [http://pdbe.org/6jbc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jbc RCSB], [http://www.ebi.ac.uk/pdbsum/6jbc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jbc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/POK_THEKO POK_THEKO]] Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in the CoA biosynthesis pathway (PubMed:19666462, PubMed:22865846). Displays broad nucleotide specificity and utilizes ATP, GTP, UTP, and CTP with comparable catalytic efficiencies (PubMed:22865846).<ref>PMID:19666462</ref> <ref>PMID:22865846</ref>
[[http://www.uniprot.org/uniprot/POK_THEKO POK_THEKO]] Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in the CoA biosynthesis pathway (PubMed:19666462, PubMed:22865846). Displays broad nucleotide specificity and utilizes ATP, GTP, UTP, and CTP with comparable catalytic efficiencies (PubMed:22865846).<ref>PMID:19666462</ref> <ref>PMID:22865846</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The coenzyme A biosynthesis pathways in most archaea involve two unique enzymes, pantoate kinase and phosphopantothenate synthetase, to convert pantoate to 4'-phosphopantothenate. Here, we report the first crystal structure of pantoate kinase from the hyperthermophilic archaeon, Thermococcus kodakarensis and its complex with ATP and a magnesium ion. The electron density for the adenosine moiety of ATP was very weak, which most likely relates to its broad nucleotide specificity. Based on the structure of the active site that contains a glycerol molecule, the pantoate binding site and the roles of the highly conserved residues are suggested.
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Crystal structure of pantoate kinase from Thermococcus kodakarensis.,Kita A, Kishimoto A, Shimosaka T, Tomita H, Yokooji Y, Imanaka T, Atomi H, Miki K Proteins. 2020 May;88(5):718-724. doi: 10.1002/prot.25852. Epub 2019 Nov 20. PMID:31697438<ref>PMID:31697438</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 6jbc" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 06:28, 19 August 2020

Phosphotransferase related to CoA biosynthesis pathway

PDB ID 6jbc

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