Crystal Structure of Asparagine Synthetase Reveals a Close Evolutionary Relationship to Class II Aminoacyl-tRNA Synthetase (MOLECULAR BIOFUNCTION-Functional Molecular Conversion)

• Nakatsu, Toru

• Kato, Hiroaki

• Oda, Jun'ichi

抄録

The crystal structure of E. coli asparagine synthetase has been determined by X-ray diffraction analysis at 2.5 A resolution. The overall structure of the enzyme is remarkably similar to that of the catalytic domain of yeast aspartyl-tRNA synthetase despite low sequence similarity. These enzymes have a common reaction mechanism that implies the formation of aminoacyl-adenylate intermediate. The active site architecture and most of the catalytic residues are also conserved in both enzymes. These enzymes have probably evolved from a common ancestor even though their sequence similarities are small.

収録刊行物

• ICR Annual Report

  ICR Annual Report 4 44-45, 1998-03

  Institute for Chemical Research, Kyoto University

キーワード

• X-ray crystallography
• Evolution
• Structural similarity
• Aspartyl-tRNA synthetase
• Amino acyl-adenylate intermediate
• Enzymatic reaction

詳細情報

• CRID: 1050001335568156160
• NII論文ID: 120000885601
• NII書誌ID: AA11061308
• ISSN: 13420321
• HANDLE: 2433/65146
• 本文言語コード: en
• 資料種別: article
• データソース種別:
  • IRDB
  • CiNii Articles