4jk3: Difference between revisions

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New page: '''Unreleased structure''' The entry 4jk3 is ON HOLD Authors: Quitterer, F., Beck, P., Bacher, A., Groll, M. Description: PylD holoenzyme (SeMet)
 
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'''Unreleased structure'''


The entry 4jk3 is ON HOLD
==PylD holoenzyme (SeMet)==
<StructureSection load='4jk3' size='340' side='right'caption='[[4jk3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4jk3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_barkeri_str._Fusaro Methanosarcina barkeri str. Fusaro]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JK3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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=4jk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jk3 OCA], [https://pdbe.org/4jk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jk3 RCSB], [https://www.ebi.ac.uk/pdbsum/4jk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jk3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PYLD_METBF PYLD_METBF] Catalyzes the ultimate step of the pyrrolysine biosynthesis pathway by converting the isopeptide (3R)-3-methyl-D-ornithyl-N(6)-L-lysine to the 22nd proteinogenic amino acid (PubMed:24916332). Is able to use surrogate substrates such as (3R)-D-ornithyl-N(6)-L-lysine in vitro (PubMed:23720358, PubMed:24916332).<ref>PMID:23720358</ref> <ref>PMID:24916332</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The final step in the biosynthesis of the 22nd genetically encoded amino acid, pyrrolysine, is catalyzed by PylD, a structurally and mechanistically unique dehydrogenase. This catalyzed reaction includes an induced-fit mechanism achieved by major structural rearrangements of the N-terminal helix upon substrate binding. Different steps of the reaction trajectory are visualized by complex structures of PylD with substrate and product.


Authors: Quitterer, F., Beck, P., Bacher, A., Groll, M.
Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD).,Quitterer F, Beck P, Bacher A, Groll M Angew Chem Int Ed Engl. 2013 May 29. doi: 10.1002/anie.201301164. PMID:23720358<ref>PMID:23720358</ref>


Description: PylD holoenzyme (SeMet)
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4jk3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanosarcina barkeri str. Fusaro]]
[[Category: Bacher A]]
[[Category: Beck P]]
[[Category: Groll M]]
[[Category: Quitterer F]]

Latest revision as of 11:01, 6 November 2024

PylD holoenzyme (SeMet)

4jk3, resolution 2.50Å

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