Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet - PubMed (original) (raw)
Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet
E Schmitt et al. EMBO J. 1998.
Abstract
The crystal structure of Escherichia coli methionyl-tRNAfMet transformylase complexed with formyl-methionyl-tRNAfMet was solved at 2.8 A resolution. The formylation reaction catalyzed by this enzyme irreversibly commits methionyl-tRNAfMet to initiation of translation in eubacteria. In the three-dimensional model, the methionyl-tRNAfMet formyltransferase fills in the inside of the L-shaped tRNA molecule on the D-stem side. The anticodon stem and loop are away from the protein. An enzyme loop is wedged in the major groove of the acceptor helix. As a result, the C1-A72 mismatch characteristic of the initiator tRNA is split and the 3' arm bends inside the active centre. This recognition mechanism is markedly distinct from that of elongation factor Tu, which binds the acceptor arm of aminoacylated elongator tRNAs on the T-stem side.
Similar articles
- Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNAMet(f) formyltransferase complexed with formyl-methionyl-tRNAMet(f).
Schmitt E, Blanquet S, Mechulam Y. Schmitt E, et al. Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):332-4. doi: 10.1107/S0907444998011780. Epub 1999 Jan 1. Acta Crystallogr D Biol Crystallogr. 1999. PMID: 10089442 - Recognition of the initiator tRNA by the Pseudomonas aeruginosa methionyl-tRNA formyltransferase: importance of the base-base mismatch at the end of the acceptor stem.
Newton DT, Niemkiewicz M, Lo RY, Mangroo D. Newton DT, et al. FEMS Microbiol Lett. 1999 Sep 15;178(2):289-98. doi: 10.1111/j.1574-6968.1999.tb08690.x. FEMS Microbiol Lett. 1999. PMID: 10499278 - RNA-protein complexes.
Cusack S. Cusack S. Curr Opin Struct Biol. 1999 Feb;9(1):66-73. doi: 10.1016/s0959-440x(99)80009-8. Curr Opin Struct Biol. 1999. PMID: 10400475 Review. - Escherichia coli initiator tRNA: structure-function relationships and interactions with the translational machinery.
Mangroo D, Wu XQ, RajBhandary UL. Mangroo D, et al. Biochem Cell Biol. 1995 Nov-Dec;73(11-12):1023-31. doi: 10.1139/o95-109. Biochem Cell Biol. 1995. PMID: 8722017 Review.
Cited by
- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.
Sigal M, Matsumoto S, Beattie A, Katoh T, Suga H. Sigal M, et al. Chem Rev. 2024 May 22;124(10):6444-6500. doi: 10.1021/acs.chemrev.3c00894. Epub 2024 Apr 30. Chem Rev. 2024. PMID: 38688034 Review. - Systematic identification and characterization of genes in the regulation and biogenesis of photosynthetic machinery.
Kafri M, Patena W, Martin L, Wang L, Gomer G, Ergun SL, Sirkejyan AK, Goh A, Wilson AT, Gavrilenko SE, Breker M, Roichman A, McWhite CD, Rabinowitz JD, Cross FR, Wühr M, Jonikas MC. Kafri M, et al. Cell. 2023 Dec 7;186(25):5638-5655.e25. doi: 10.1016/j.cell.2023.11.007. Cell. 2023. PMID: 38065083 Free PMC article. - Investigation of the Importance of Protein 3D Structure for Assessing Conservation of Lysine Acetylation Sites in Protein Homologs.
Jew KM, Le VTB, Amaral K, Ta A, Nguyen May NM, Law M, Adelstein N, Kuhn ML. Jew KM, et al. Front Microbiol. 2022 Jan 31;12:805181. doi: 10.3389/fmicb.2021.805181. eCollection 2021. Front Microbiol. 2022. PMID: 35173693 Free PMC article. - Structure of putative tumor suppressor ALDH1L1.
Tsybovsky Y, Sereda V, Golczak M, Krupenko NI, Krupenko SA. Tsybovsky Y, et al. Commun Biol. 2022 Jan 10;5(1):3. doi: 10.1038/s42003-021-02963-9. Commun Biol. 2022. PMID: 35013550 Free PMC article. - Towards Engineering an Orthogonal Protein Translation Initiation System.
Lee BS, Choi WJ, Lee SW, Ko BJ, Yoo TH. Lee BS, et al. Front Chem. 2021 Oct 26;9:772648. doi: 10.3389/fchem.2021.772648. eCollection 2021. Front Chem. 2021. PMID: 34765589 Free PMC article.
References
- Biochemistry. 1985 Dec 3;24(25):7309-14 - PubMed
- Proc Natl Acad Sci U S A. 1997 Dec 9;94(25):13524-9 - PubMed
- FEBS Lett. 1973 Mar 15;30(3):291-5 - PubMed
- Nature. 1974 Mar 1;248(5443):20-4 - PubMed
- Proc Natl Acad Sci U S A. 1975 Nov;72(11):4414-8 - PubMed
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials