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Crystal structure of Streptococcus pneumoniae Sp1610, a putative tRNA methyltransferase, in complex with

Hai Minh Ta1, Kyeong Kyu Kim

  • 1Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea.

Protein Science : a Publication of the Protein Society
|January 7, 2010
PubMed

Insights

This study reveals the crystal structure of Streptococcus pneumoniae Sp1610, an S-adenosylmethionine-dependent methyltransferase. Structural analysis identified key features for bacterial tRNA methylation and substrate recognition.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Streptococcus pneumoniae Sp1610 is a Class-I S-adenosylmethionine (AdoMet)-dependent methyltransferase.
  • It belongs to the COG2384 family and methylates bacterial tRNA at N(1)-adenosine position 22.

Purpose of the Study:

  • To determine the crystal structure of Sp1610 in ligand-free and AdoMet-bound states.
  • To elucidate the structural basis for its methyltransferase activity and substrate recognition.

Main Methods:

  • X-ray crystallography to obtain structures at 2.0 and 3.0 Å resolution.
  • Sequence alignment and structural analysis.

Main Results:

  • The crystal structure reveals Sp1610 comprises an N-terminal catalytic domain and a novel C-terminal substrate recognition domain.
  • Electrostatic potential mapping identified a positively charged RNA binding area near the AdoMet pocket.
  • Putative catalytic residues for substrate recognition were proposed.

Conclusions:

  • The determined structures provide insights into the mechanism of bacterial tRNA methylation by Sp1610.
  • The findings contribute to understanding methyltransferase function and substrate interaction in bacteria.

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