Crystal structure of serine dehydrogenase from Escherichia coli : important role of the C-terminal region for closed-complex formation

この論文にアクセスする

この論文をさがす

著者

抄録

Serine dehydrogenase from Escherichia coli is a homotetrameric enzyme belonging to the short-chain dehydrogenase/reductase (SDR) family. This enzyme catalyses the NADP(+)-dependent oxidation of serine to 2-aminomalonate semialdehyde. The enzyme shows a stereospecificity for β-(3S)-hydroxy acid as a substrate; however, no stereospecificity was observed at the α-carbon. The structures of the ligand-free SerDH and SerDH-NADP(+)-phosphate complex were determined at 1.9 and 2.7 Å resolutions, respectively. The overall structure, including the catalytic tetrad of Asn106, Ser134, Tyr147 and Lys151, shows obvious relationships with other members of the SDR family. The structure of the substrate-binding loop and that of the C-terminal region were disordered in the ligand-free enzyme, whereas these structures were clearly defined in the SerDH-NADP(+) complex as a closed form. Interestingly, the C-terminal region was protruded from the main body and it formed an anti-parallel β-sheet with another C-terminal region on the subunit that is diagonally opposite to that in the tetramer. It is revealed that the C-terminal region possesses the important roles in substrate binding through the stabilization of the substrate-binding loop in the closed form complex. The roles of the C-terminal region along with those of the residues involved in substrate recognition were studied by site-directed mutagenesis.

収録刊行物

  • The journal of biochemistry

    The journal of biochemistry 149(6), 701-712, 2011-06-01

    Japanese Biochemical Society

参考文献:  25件中 1-25件 を表示

各種コード

  • NII論文ID(NAID)
    10030585881
  • NII書誌ID(NCID)
    AA00694073
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    0021924X
  • NDL 記事登録ID
    11100503
  • NDL 雑誌分類
    ZR2(科学技術--生物学--生化学)
  • NDL 請求記号
    Z53-B472
  • データ提供元
    CJP書誌  NDL  IR 
ページトップへ