The structure and function of the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Haemophilus influenzae
The structure and function of the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Haemophilus influenzae
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DOI：
10.1006/jmbi.1999.2623
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发表时间：
1999-03-26
影响因子：
5.6
通讯作者：
Oefner, C
中科院分区：
文献类型：
--
作者：
Hennig, M;Dale, GE;Oefner, C
流感嗜血杆菌6-羟甲基-7，8-二氢蝶呤焦磷酸激酶基因已克隆并在大肠杆菌中表达。纯化的蛋白质与底物类似物的复合物已经结晶，其结构通过使用从硒代甲硫氨酸标记的蛋白质的单晶获得的相位信息的多重异常分散来解决。该酶折叠成一个四链反平行β-折叠，一侧为两个α-螺旋，另一侧为三个连续的α-螺旋，得到一种新的β（1）α（1）β（2）β（3）α（2）β（4）α（3）α（4）α（5）多肽拓扑结构。一个二元复合物的三维结构已经在2.1埃分辨率下得到了改进。底物类似物和硫酸根离子的位置提供了重要的洞察酶的分子机制。(C)北京：科学出版社.
The gene encoding the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase of Haemophilus influenzae has been cloned and expressed in Escherichia coli. A complex of the purified protein with a substrate analog has been crystallized and its structure solved by multiple anomalous dispersion using phase information obtained from a single crystal of selenomethione-labeled protein. The enzyme folds into a four-stranded antiparallel beta-sheet flanked on one side by two alpha-helices and on the other by three consecutive alpha-helices, giving a novel beta(1)alpha(1)beta(2)beta(3)alpha(2)beta(4)alpha(3)alpha(4)alpha(5) polypeptide topology. The three-dimensional structure of a binary complex has been refined at 2.1 Angstrom resolution. The location of the substrate analog and a sulfate ion gives important insight into the molecular mechanism of the enzyme. (C) 1999 Academic Press.