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Purification of a High Molecular Mass Protein in Streptococcus mutans
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Purification of a High Molecular Mass Protein in Streptococcus mutans

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The structure of the hypothetical protein smu.1377c from Streptococcus mutans suggests a role in tRNA modification

Tian Min Fu1, Xiang Liu, Lanfen Li

  • 1The National Laboratory of Protein Engineering and Plant Genetic Engineering, School of Life Sciences, Peking University, Beijing 100871, People's Republic of China.

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
|July 8, 2010
PubMed

Insights

Streptococcus mutans smu.1377c protein belongs to the Sua5_YciO_YrdC family. Structural analysis suggests it may function similarly to Escherichia coli YrdC in tRNA modification.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • The Sua5_YciO_YrdC protein family is conserved across eukaryotes and prokaryotes.
  • These proteins share a common alpha/beta twisted open-sheet fold.
  • The Escherichia coli YrdC protein is known to be involved in tRNA modification.

Purpose of the Study:

  • To determine the crystal structure of the hypothetical protein smu.1377c from Streptococcus mutans.
  • To analyze the structure of smu.1377c and compare it to known proteins in the Sua5_YciO_YrdC family.

Main Methods:

  • X-ray crystallography was used to determine the structure of smu.1377c.
  • Structural analysis and comparative studies were performed.

Main Results:

  • The crystal structure of smu.1377c was determined to a resolution of 2.25 Å.
  • Structural analysis confirmed smu.1377c as a member of the Sua5_YciO_YrdC protein family.

Conclusions:

  • The hypothetical protein smu.1377c from Streptococcus mutans shares structural homology with the Sua5_YciO_YrdC family.
  • Based on structural similarity, smu.1377c is proposed to have a similar function to E. coli YrdC, potentially in tRNA modification.

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