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

被引:26
作者
Andersson, A
Jordan, D
Schneider, G
Lindqvist, Y
机构
[1] KAROLINSKA INST,DEPT MED BIOCHEM & BIOPHYS,S-17177 STOCKHOLM,SWEDEN
[2] SWEDISH UNIV AGR SCI,UPPSALA BIOMED CTR,DEPT MOL BIOL,S-75124 UPPSALA,SWEDEN
[3] DUPONT CO INC,STINE HASKELL RES CTR,AGR PROD,NEWARK,DE 19714
关键词
rice blast; naphthol reductase; protein crystallography; short-chain dehydrogenase;
D O I
10.1016/S0014-5793(96)01382-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The crystal structures of apo-1,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea and a binary complex of the enzyme with NADPH have been determined to 2.8 Angstrom 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.
引用
收藏
页码:173 / 176
页数:4
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