Journal of the Korean Magnetic Resonance Society (한국자기공명학회논문지)
- Volume 9 Issue 2
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- Pages.110-121
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- 2005
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- 1226-6531(pISSN)
Structural Studies on the E. coli Methionyl-tRNA Synthetase and Their Interaction with E. coli $tRNA^{fMet}$
- Kim Ji-Hun (Research Institute of Pharmaceutical sciences, College of Pharmacy, Seoul National University) ;
- Ahn Hee-Chul (Research Institute of Pharmaceutical sciences, College of Pharmacy, Seoul National University) ;
- Park Sung-Jin (Research Institute of Pharmaceutical sciences, College of Pharmacy, Seoul National University) ;
- Kim Sung-Hoon (Research Institute of Pharmaceutical sciences, College of Pharmacy, Seoul National University) ;
- Lee Bong-Jin (Research Institute of Pharmaceutical sciences, College of Pharmacy, Seoul National University)
- Published : 2005.12.01
Abstract
E.coli methionyl tRNA synthetase consist of 676 amino acids and plays a key role in initiation of protein synthesis. The native form of this enzyme is a homodimer, but the monomeric enzyme truncated approximately C-terminal 120 amino acids retains the full enzymatic activities. X-ray crystal structure of the active monomeric enzyme shows that it has two domains. The N-terminal domain is thought to be a binding site for acceptor stem of tRNA, ATP, and methionine. The C-terminal domain is mainly a-helical and makes an interaction with the anticodon of
Keywords
- methionyl-tRNA synthetase;
- $tRNA^{Met}$;
- anticodon;
- NMR;
- circular dichroism;
- fluorescence;
- protein-tRNA interaction