A flexible lid controls access to the active site in 1,3,8‐trihydroxynaphthalene reductase

FEBS Letters

Lindqvist, Ylva²  Andersson, Arnold³  Schneider, Gunter²  Jordan, Douglas¹ 

[1] Dupont Agricultural Products, Stine-Haskell Research Center, Box 30, Elkton Road, Newark, DE 19714, USA;Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77 Stockholm, Sweden;Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, PO Box 590, S-75124 Uppsala, Sweden

关键词: Rice blast;    Naphtol reductase;    Protein crystallography;    Short-chain dehydrogenase;    THNR;    1;    3;    8-trihydroxynaphthalene reductase;   

DOI  :  10.1016/S0014-5793(96)01382-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The crystal structures of apo-1,3,8-trihydroxy-naphthalene reductase from Magnaporthe grisea and a binary complex of the enzyme with NADPH have been determined to 2.8 Å resolution. In both cases, the overall structure is preserved compared to the structure of the ternary complex of the enzyme with NADPH and an active site inhibitor. No electron density for the helix–loop–helix region comprising residues 214–244 is observed indicating structural disorder in this part of the apoenzyme and the binary complex. In the ternary complex, this region is in contact with NADPH and the inhibitor and closes off the active site. The observed increase in flexibility in the absence of the inhibitor indicates that this region acts as a lid which closes the active site upon binding of the inhibitor and, possibly the substrate, 1,3,8-trihydroxynaphthalene.

【 授权许可】

Unknown