6ia8: Difference between revisions

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==Apo crystal structure of archaeal Methanocaldococcus infernus Elp3 (del1-19)==
==Apo crystal structure of archaeal Methanocaldococcus infernus Elp3 (del1-19)==
<StructureSection load='6ia8' size='340' side='right' caption='[[6ia8]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='6ia8' size='340' side='right'caption='[[6ia8]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ia8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IA8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IA8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6ia8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_infernus Methanocaldococcus infernus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IA8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<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=6ia8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ia8 OCA], [http://pdbe.org/6ia8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ia8 RCSB], [http://www.ebi.ac.uk/pdbsum/6ia8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ia8 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=6ia8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ia8 OCA], [https://pdbe.org/6ia8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ia8 RCSB], [https://www.ebi.ac.uk/pdbsum/6ia8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ia8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ELP3_METIM ELP3_METIM] tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:25151136, PubMed:30733442). The proposed mechanism is the following: (i) recruits S-adenosyl-L-methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'-dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule (PubMed:25151136). Does not show protein lysine acetyltransferase activity (PubMed:30733442).<ref>PMID:25151136</ref> <ref>PMID:30733442</ref>
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6ia8" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6ia8" style="background-color:#fffaf0;"></div>
==See Also==
*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Histone acetyltransferase]]
[[Category: Large Structures]]
[[Category: Glatt, S]]
[[Category: Methanocaldococcus infernus]]
[[Category: Lin, T Y]]
[[Category: Glatt S]]
[[Category: Acetyl-coa hydrolysis]]
[[Category: Lin TY]]
[[Category: Elongator complex]]
[[Category: Non-canonical acetyltransferase]]
[[Category: Transferase]]
[[Category: Trna binding]]

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