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首页> 外文期刊>Acta crystallographica. Section D, Structural biology >Crystallographic binding studies of rat peroxisomal multifunctional enzyme type 1 with 3-ketodecanoyl-CoA: capturing active and inactive states of its hydratase and dehydrogenase catalytic sites
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Crystallographic binding studies of rat peroxisomal multifunctional enzyme type 1 with 3-ketodecanoyl-CoA: capturing active and inactive states of its hydratase and dehydrogenase catalytic sites

机译：研究大鼠晶体绑定过氧化物酶病1型多功能酶3-ketodecanoyl-CoA:捕捉活跃的和不活跃的州的水合酶和脱氢酶催化网站

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摘要

The peroxisomal multifunctional enzyme type 1 (MFE1) catalyzes two successive reactions in the /3-oxidation cycle: the 2E-enoyl-CoA hydratase (ECH) and NAD+-dependent 3S-hydroxyacyl-CoA dehydrogenase (HAD) reactions. MFE1 is a monomeric enzyme that has five domains. The N-terminal part (domains A and B) adopts the crotonase fold and the C-terminal part (domains C, D and E) adopts the HAD fold. A new crystal form of MFE1 has captured a conformation in which both active sites are noncompetent. This structure, at 1.7 A resolution, shows the importance of the interactions between Phe272 in domain B (the linker helix; helix H10 of the crotonase fold) and the beginning of loop 2 (of the crotonase fold) in stabilizing the competent ECH active-site geometry. In addition, protein crystallographic binding studies using optimized crystal-treatment protocols have captured a structure with both the 3-ketodecanoyl-CoA product and NAD+ bound in the HAD active site, showing the interactions between 3-ketodecanoyl-CoA and residues of the C, D and E domains. Structural comparisons show the importance of domain movements, in particular of the C domain with respect to the D/E domains and of the A domain with respect to the HAD part. These comparisons suggest that the N-terminal part of the linker helix, which interacts tightly with domains A and E, functions as a hinge region for movement of the A domain with respect to the HAD part.
机译：过氧化物酶病多功能酶1型(MFE1)催化两个连续反应/三氧化二铝周期:2 e-enoyl-coa水合酶(决定)和NAD + 3 s-hydroxyacyl-coa端依赖脱氢酶(已经)反应。单体的酶,有五个领域。氨基端部分(域A和B)采用crotonase褶皱和c端部分(域C、D、E)采用了褶皱。形式的MFE1的构象活跃的站点都是noncompetent。结构,在1.7一项决议,显示了Phe272之间的相互作用的重要性域B(链接器螺旋;crotonase褶皱)和2(循环的开始crotonase褶皱)在稳定能力决定活性部位的几何形状。晶体绑定使用优化的研究crystal-treatment协议已抓获结构与3-ketodecanoyl-CoA产品和NAD +绑定的活性部位,显示之间的交互3-ketodecanoyl-CoA和残留的C, D和E域。域运动的重要性,特别是C域的域和D / E的一个域的一部分。这些比较表明,氨基链接器螺旋的一部分,紧密交互域和E,函数作为枢纽区域的运动的有一部分。

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