Crystal Structure of catalytic fragment of E. coli AlaRS G237A in complex with GlySACrystal Structure of catalytic fragment of E. coli AlaRS G237A in complex with GlySA
Structural highlights
3hy0 is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
SYA_ECOLI Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). AlaRS also incorrectly activates the sterically smaller than alanine amino acid glycine as well as the sterically larger amino acid serine. These incorrectly charged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (glycine and serine) in the charging step.[1][2][3] Edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) but not incorrectly charged Ser-tRNA(Thr).[4][5][6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Beebe K, Ribas De Pouplana L, Schimmel P. Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability. EMBO J. 2003 Feb 3;22(3):668-75. PMID:12554667 doi:10.1093/emboj/cdg065
↑Chong YE, Yang XL, Schimmel P. Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation. J Biol Chem. 2008 Oct 31;283(44):30073-8. doi: 10.1074/jbc.M805943200. Epub 2008 , Aug 22. PMID:18723508 doi:10.1074/jbc.M805943200
↑Guo M, Chong YE, Beebe K, Shapiro R, Yang XL, Schimmel P. The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science. 2009 Aug 7;325(5941):744-7. PMID:19661429 doi:325/5941/744
↑Beebe K, Ribas De Pouplana L, Schimmel P. Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability. EMBO J. 2003 Feb 3;22(3):668-75. PMID:12554667 doi:10.1093/emboj/cdg065
↑Chong YE, Yang XL, Schimmel P. Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation. J Biol Chem. 2008 Oct 31;283(44):30073-8. doi: 10.1074/jbc.M805943200. Epub 2008 , Aug 22. PMID:18723508 doi:10.1074/jbc.M805943200
↑Guo M, Chong YE, Beebe K, Shapiro R, Yang XL, Schimmel P. The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science. 2009 Aug 7;325(5941):744-7. PMID:19661429 doi:325/5941/744
