4hjr: Difference between revisions

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{{STRUCTURE_4hjr|  PDB=4hjr  |  SCENE=  }}
===Crystal structure of F2YRS===
{{ABSTRACT_PUBMED_23450644}}


==About this Structure==
==Crystal structure of F2YRS==
[[4hjr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_dsm_2661 Methanocaldococcus jannaschii dsm 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HJR OCA].  
<StructureSection load='4hjr' size='340' side='right'caption='[[4hjr]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
[[Category: Methanocaldococcus jannaschii dsm 2661]]
== Structural highlights ==
[[Category: Tyrosine--tRNA ligase]]
<table><tr><td colspan='2'>[[4hjr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HJR FirstGlance]. <br>
[[Category: Ding, W.]]
</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>
[[Category: Gong, W.]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4hjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hjr OCA], [https://pdbe.org/4hjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hjr RCSB], [https://www.ebi.ac.uk/pdbsum/4hjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hjr ProSAT]</span></td></tr>
[[Category: Li, F.]]
</table>
[[Category: Li, J.]]
== Function ==
[[Category: Shi, P.]]
[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>
[[Category: Tian, C.]]
<div style="background-color:#fffaf0;">
[[Category: Wang, J.]]
== Publication Abstract from PubMed ==
[[Category: Aminoacyl-trna synthetase]]
Simple and selective: Tyrosine phosphorylation is a pivotal post-translational modification which regulates the enzymatic activity, protein conformation, and protein-protein interactions. The highly efficient genetic incorporation of 3,5-difluorotyrosine (F2Y) in E. coli and the use of F2Y as a 19 F NMR probe for the tyrosine phosphorylation are reported.
[[Category: F2y]]
 
[[Category: Ligase]]
A Genetically Encoded F NMR Probe for Tyrosine Phosphorylation.,Li F, Shi P, Li J, Yang F, Wang T, Zhang W, Gao F, Ding W, Li D, Li J, Xiong Y, Sun J, Gong W, Tian C, Wang J Angew Chem Int Ed Engl. 2013 Feb 28. doi: 10.1002/anie.201300463. PMID:23450644<ref>PMID:23450644</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4hjr" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanocaldococcus jannaschii DSM 2661]]
[[Category: Ding W]]
[[Category: Gong W]]
[[Category: Li F]]
[[Category: Li J]]
[[Category: Shi P]]
[[Category: Tian C]]
[[Category: Wang J]]

Latest revision as of 18:07, 20 September 2023

Crystal structure of F2YRSCrystal structure of F2YRS

Structural highlights

4hjr is a 2 chain structure with sequence from Methanocaldococcus jannaschii DSM 2661. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
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]

Publication Abstract from PubMed

Simple and selective: Tyrosine phosphorylation is a pivotal post-translational modification which regulates the enzymatic activity, protein conformation, and protein-protein interactions. The highly efficient genetic incorporation of 3,5-difluorotyrosine (F2Y) in E. coli and the use of F2Y as a 19 F NMR probe for the tyrosine phosphorylation are reported.

A Genetically Encoded F NMR Probe for Tyrosine Phosphorylation.,Li F, Shi P, Li J, Yang F, Wang T, Zhang W, Gao F, Ding W, Li D, Li J, Xiong Y, Sun J, Gong W, Tian C, Wang J Angew Chem Int Ed Engl. 2013 Feb 28. doi: 10.1002/anie.201300463. PMID:23450644[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
  2. Li F, Shi P, Li J, Yang F, Wang T, Zhang W, Gao F, Ding W, Li D, Li J, Xiong Y, Sun J, Gong W, Tian C, Wang J. A Genetically Encoded F NMR Probe for Tyrosine Phosphorylation. Angew Chem Int Ed Engl. 2013 Feb 28. doi: 10.1002/anie.201300463. PMID:23450644 doi:10.1002/anie.201300463

4hjr, resolution 2.50Å

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