3d6v: Difference between revisions

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<StructureSection load='3d6v' size='340' side='right'caption='[[3d6v]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3d6v' size='340' side='right'caption='[[3d6v]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3d6v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2q1i 2q1i]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D6V FirstGlance]. <br>
<table><tr><td colspan='2'>[[3d6v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2q1i 2q1i]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D6V FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=TFQ:4-(2,2,2-TRIFLUOROETHYL)-L-PHENYLALANINE'>TFQ</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]] 2.2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1j1u|1j1u]], [[3d6u|3d6u]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=TFQ:4-(2,2,2-TRIFLUOROETHYL)-L-PHENYLALANINE'>TFQ</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tyrS, MJ0389 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] </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=3d6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d6v OCA], [https://pdbe.org/3d6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d6v RCSB], [https://www.ebi.ac.uk/pdbsum/3d6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d6v 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=3d6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d6v OCA], [https://pdbe.org/3d6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d6v RCSB], [https://www.ebi.ac.uk/pdbsum/3d6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d6v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SYY_METJA SYY_METJA]] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).<ref>PMID:10585437</ref>
[https://www.uniprot.org/uniprot/SYY_METJA SYY_METJA] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).<ref>PMID:10585437</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43067]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Tyrosine--tRNA ligase]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Liu, W]]
[[Category: Liu W]]
[[Category: Mack, A V]]
[[Category: Mack AV]]
[[Category: Schultz, P G]]
[[Category: Schultz PG]]
[[Category: Tippmann, E]]
[[Category: Tippmann E]]
[[Category: Aminoacyl-trna synthetase]]
[[Category: Atp-binding]]
[[Category: Cytoplasm]]
[[Category: Ligase]]
[[Category: Nucleotide-binding]]
[[Category: Photocrosslinking unnatural amino acid]]
[[Category: Protein biosynthesis]]

Latest revision as of 12:40, 21 February 2024

Crystal structure of 4-(trifluoromethyldiazirinyl)phenylalanyl-tRNA synthetaseCrystal structure of 4-(trifluoromethyldiazirinyl)phenylalanyl-tRNA synthetase

Structural highlights

3d6v is a 1 chain structure with sequence from Methanocaldococcus jannaschii. This structure supersedes the now removed PDB entry 2q1i. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SYY_METJA Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Steer BA, Schimmel P. Major anticodon-binding region missing from an archaebacterial tRNA synthetase. J Biol Chem. 1999 Dec 10;274(50):35601-6. PMID:10585437

3d6v, resolution 2.20Å

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