Structural and biochemical studies of thermus thermophilusl11 trimethyltranferase (Prma) methylation of ribosomalprotein l11
Başlık çevirisi mevcut değil.
- Tez No: 611633
- Danışmanlar: PROF. DR. DANIŞMAN YOK
- Tez Türü: Doktora
- Konular: Biyokimya, Biyomühendislik, Biochemistry, Bioengineering
- Anahtar Kelimeler: Belirtilmemiş.
- Yıl: 2008
- Dil: İngilizce
- Üniversite: Brown University
- Enstitü: Yurtdışı Enstitü
- Ana Bilim Dalı: Belirtilmemiş.
- Bilim Dalı: Belirtilmemiş.
- Sayfa Sayısı: 217
Özet
Bacterial ribosomal protein L11 is a universally conserved component of the large subunit, and plays a significant role during initiation, elongation, and termination of protein synthesis. L11 protein is post-translationally trimethylated at multiple residues by a single methyltransferase, PrmA. In Escherichia coli, the lysine methyltransferase PrmA trimethylates the N-terminal α-amino group and the ɛamino groups of Lys3 and Lys39. In this thesis, I describe multiple structures of PrmA from the extreme thermophile Thermus thermophilus. Two apo-PrmA structures at 1.59 and 2.3 Å resolution and a third with bound cofactor AdoMet at 1.75 Å each exhibit distinct relative positions of the substrate recognition and catalytic domains, revealing how PrmA can position the L11 substrate for multiple, consecutive side-chain methylation reactions. The fourth structure, the PrmA–L11 enzyme–substrate complex at 2.4 Å resolution, illustrates the highly specific interaction of the N-terminal domain with its substrate and places Lys39 in the PrmA active site. The presence of a unique flexible loop in the cofactor-binding site suggests how exchange of AdoMet with the reaction product AdoHcy can occur without necessitating the dissociation of PrmA from L11. The mode of interaction of PrmA with L11 explains its observed preference for L11 as substrate before its assembly into the 50S ribosomal subunit. I also report four catalytic PrmA-L11 complex structures in different orientations with respect to the PrmA active site. Two structures capture the L11 N-terminal α-amino group in the active site in a trimethylated postcatalytic state and in a dimethylated state with bound AdoHcy. Two other structures show L11 in a catalytic orientation to modify Lys39 and in a noncatalytic orientation. The comparison of complex structures in different orientations with a minimal substrate recognition complex shows that the binding mode remains conserved in all L11 orientations, and that substrate orientation is brought about by the unusual interdomain flexibility of PrmA. Collectively, the structures presented in this thesis explains the underpinnings of recognition and catalysis of this fascinating enzyme-substrate complex.
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