Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp strain RHA1
Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp strain RHA1
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DOI：
10.1016/j.jmb.2004.07.062
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发表时间：
2004-09-17
影响因子：
5.6
通讯作者：
Senda, T
中科院分区：
文献类型：
--
作者：
Furusawa, Y;Nagarajan, V;Senda, T
联苯双加氧酶是一种催化芳环立体定向双加氧的酶。多氯联苯是一种严重的环境污染物，该酶对多氯联苯的氧化能力引起了研究者的关注。我们测定了红球菌联苯双加氧酶(BphA1A2)末端加氧酶组分的晶体结构。RHA1以无底物和复杂形式存在。这些晶体结构表明，底物结合口袋在底物结合时发生了显著的构象变化，以将底物容纳到口袋中。我们对晶体结构的分析表明，底物结合袋中的残基可以分为三类，分别与催化反应、底物的取向/构象和底物结合袋的构象变化有关。三组残基的协同作用似乎决定了该酶的底物专一性。(C)2004爱思唯尔有限公司。保留所有权利。
Biphenyl dioxygenase is the enzyme that catalyzes the stereospecific dioxygenation of the aromatic ring. This enzyme has attracted the attention of researchers due to its ability to oxidize polychlorinated biphenyls, which is one of the serious environmental contaminants. We determined the crystal structure of the terminal oxygenase component of the biphenyl dioxygenase (BphA1A2) derived from Rhodococcus strain sp. RHA1 in substrate-free and complex forms. These crystal structures revealed that the substrate-binding pocket makes significant conformational changes upon substrate binding to accommodate the substrate into the pocket. Our analysis of the crystal structures suggested that the residues in the substrate-binding pocket can be classified into three groups, which, respectively, seem to be responsible for the catalytic reaction, the orientation/conformation of the substrate, and the conformational changes of the substrate-binding pocket. The cooperative actions of residues in the three groups seem to determine the substrate specificity of the enzyme. (C) 2004 Elsevier Ltd. All rights reserved.