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4j49

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==PylD holoenzyme soaked with L-lysine-Ne-D-ornithine==
==PylD holoenzyme soaked with L-lysine-Ne-D-ornithine==
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<StructureSection load='4j49' size='340' side='right' caption='[[4j49]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='4j49' size='340' side='right'caption='[[4j49]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4j49]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Metbf Metbf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J49 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4j49]] 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=4J49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J49 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=1J1:N~6~-[(2R)-3,4-DIHYDRO-2H-PYRROL-2-YLCARBONYL]-L-LYSINE'>1J1</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</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]] 2.2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t7v|3t7v]], [[4ffp|4ffp]], [[4j43|4j43]], [[4j4b|4j4b]], [[4j4h|4j4h]]</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=1J1:N~6~-[(2R)-3,4-DIHYDRO-2H-PYRROL-2-YLCARBONYL]-L-LYSINE'>1J1</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mbar_A0835 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269797 METBF])</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=4j49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j49 OCA], [https://pdbe.org/4j49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j49 RCSB], [https://www.ebi.ac.uk/pdbsum/4j49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j49 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=4j49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j49 OCA], [http://pdbe.org/4j49 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j49 RCSB], [http://www.ebi.ac.uk/pdbsum/4j49 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j49 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/Q46E80_METBF Q46E80_METBF]
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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.
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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>
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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 4j49" 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: Metbf]]
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[[Category: Large Structures]]
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[[Category: Bacher, A]]
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[[Category: Methanosarcina barkeri str. Fusaro]]
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[[Category: Beck, P]]
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[[Category: Bacher A]]
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[[Category: Groll, M]]
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[[Category: Beck P]]
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[[Category: Quitterer, F]]
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[[Category: Groll M]]
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[[Category: 22nd amino acid]]
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[[Category: Quitterer F]]
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[[Category: Biosynthesis]]
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[[Category: Dehydrogenase]]
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[[Category: L-lysine-ne-3r-methyl-d-ornithine]]
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[[Category: Nad]]
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[[Category: Oxidoreductase]]
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[[Category: Pyrrolysine]]
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[[Category: Rossmann fold]]
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Current revision

PylD holoenzyme soaked with L-lysine-Ne-D-ornithine

PDB ID 4j49

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