Crystallization and preliminary X-ray analysis of the formiminotransferase domain from the bifunctional enzyme formiminotransferase-cyclodeaminase.

Kohls D; Mejia N; MacKenzie REVrielink ACroteau N

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Crystallization and preliminary X-ray analysis of the formiminotransferase domain from the bifunctional enzyme formiminotransferase-cyclodeaminase.

机译：结晶和初步的x射线分析formiminotransferase域的双功能酶formiminotransferase-cyclodeaminase。

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Formiminotransferase-cyclodeaminase (E.C. 2.1.2.5-E.C. 4.3.1.4) is a bifunctional enzyme involved in the histidine-degradation pathway which exhibits specificity for polyglutamylated folate substrates. The first function of the enzyme transfers the formimino group of formiminoglutamate to the N5 position of tetrahydrofolate, while the second function catalyses the cyclodeamination of the formimino group, yielding N5,10-methenyl-tetrahydrofolate, with efficient channeling of the intermediate between these activities. Initial studies have shown that the enzyme consists of eight identical subunits of 62 kDa each, arranged as a circular tetramer of dimers. It is this formation which results in two different dimeric interfaces, which are necessary for the two different activities. The identical subunits have been shown to consist of two domains, each of which can be obtained as dimers. The formiminotransferase domain has been crystallized in the presence of the substrate analogue folinic acid. The crystals belong to space group P212121, with unit-cell dimensions a = 64.4, b = 103.7, c = 122.3 A. Both a native data set and a mercurial derivative data set have been collected to 2.8 A resolution.

机译：Formiminotransferase-cyclodeaminase(。2.1.2.5-E.C。参与histidine-degradation通路这展览polyglutamylated特异性叶酸基质。酶转移formimino组formiminoglutamate到它们的位置tetrahydrofolate,而第二个函数催化作用的cyclodeamination formimino10-methenyl-tetrahydrofolate集团产生它们,与中间的有效引导这些活动之间的关系。表明酶由八个相同的每个子单元62 kDa,安排一个圆形四聚物的二聚体。结果在两个不同的二聚的接口,这两个不同是必要的吗活动。显示包含两个域,每个可以获得二聚体。formiminotransferase域结晶的底物类似物每天酸。单胞尺寸= 64.4,= 103.7 b, c= 122.3。导数数据集已经收集到2.8决议。

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《Acta crystallographica.Section D. Biological crystallography》 |1999年第6期|1206-1208|共3页
作者
Kohls D; Mejia N; MacKenzie REVrielink ACroteau N;
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Biochemistry Department, McIntyre Medical Sciences Building, McGill University, 3655 Drummond Street, Montreal, Quebec, H3G 1Y6, Canada.;

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正文语种英语
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Dimers; Protein Conformation; derived dataX-ray analysisCrystallographyhydroxymethyltransferases and formyltransferasesTetrahydrofolatesX-raysEnzymesCrystallization;

机译：二聚体;蛋白质构象;dataX-ray派生而来analysisCrystallographyhydroxymethyltransferases和;

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Crystallization and preliminary X-ray analysis of the formiminotransferase domain from the bifunctional enzyme formiminotransferase-cyclodeaminase.

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