3ty9

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<StructureSection load='3ty9' size='340' side='right'caption='[[3ty9]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
<StructureSection load='3ty9' size='340' side='right'caption='[[3ty9]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ty9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acet2 Acet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TY9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ty9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus_ATCC_27405 Acetivibrio thermocellus ATCC 27405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TY9 FirstGlance]. <br>
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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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr>
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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]] 3.12&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ty5|3ty5]], [[3ty8|3ty8]]</div></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cthe_2768 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=203119 ACET2])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/RNA_ligase_(ATP) RNA ligase (ATP)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.5.1.3 6.5.1.3] </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=3ty9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ty9 OCA], [https://pdbe.org/3ty9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ty9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ty9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ty9 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ty9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ty9 OCA], [https://pdbe.org/3ty9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ty9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ty9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ty9 ProSAT]</span></td></tr>
</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/A3DJ38_ACET2 A3DJ38_ACET2]
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Pnkp is the end-healing and end-sealing component of an RNA repair system present in diverse bacteria from ten different phyla. To gain insight to the mechanism and evolution of this repair system, we determined the crystal structures of the ligase domain of Clostridium thermocellum Pnkp in three functional states along the reaction pathway: apoenzyme, ligase*ATP substrate complex, and covalent ligase-AMP intermediate. The tertiary structure is composed of a classical ligase nucleotidyltransferase module that is embellished by a unique alpha-helical insert module and a unique C-terminal alpha-helical module. Structure-guided mutational analysis identified active site residues essential for ligase adenylylation. Pnkp defines a new RNA ligase family with signature structural and functional properties.
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The adenylyltransferase domain of bacterial Pnkp defines a unique RNA ligase family.,Smith P, Wang LK, Nair PA, Shuman S Proc Natl Acad Sci U S A. 2012 Feb 14;109(7):2296-301. Epub 2012 Jan 27. PMID:22308407<ref>PMID:22308407</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 3ty9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acet2]]
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[[Category: Acetivibrio thermocellus ATCC 27405]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Shuman, S]]
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[[Category: Shuman S]]
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[[Category: Smith, P]]
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[[Category: Smith P]]
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[[Category: Wang, L]]
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[[Category: Wang L]]
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[[Category: Adenylyltransferase]]
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[[Category: Dna ligase/mrna capping enzyme]]
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[[Category: Hen1]]
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[[Category: Rna ligase]]
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[[Category: Transferase]]
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Revision as of 13:43, 14 March 2024

Crystal Structure of C. Thermocellum PNKP Ligase Domain AMP-Adenylate

PDB ID 3ty9

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