4hjr

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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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