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首页> 外文期刊>Journal of Molecular Biology >Structural and functional study of a conserved region in the uncoupling protein UCP1: the three matrix loops are involved in the control of transport.
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Structural and functional study of a conserved region in the uncoupling protein UCP1: the three matrix loops are involved in the control of transport.

机译：解偶联蛋白UCP1中保守区的结构和功能研究：三个基质环参与运输的控制。

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摘要

It has been reported that the region 261-269 of the uncoupling protein from brown adipose tissue mitochondria, UCP1, has an important role in the control of its proton translocating activity. Thus the deletion of residues Phe267-Lys268-Gly269 leads to the loss of the nucleotide regulation of the protein, while the complete deletion of the segment leads to the formation of a pore. The region displays sequence homology with the DNA-binding domain of the estrogen receptor. The present report analyzes the structure, by NMR and circular dichroism, of a 20 amino acid residue peptide containing the residues of interest. We demonstrate that residues 263-268 adopt an alpha-helical structure. The helix is at the N-terminal end of the sixth transmembrane domain. The functional significance of this helix has been examined by site-directed mutagenesis of the protein expressed recombinantly in yeasts. Alterations in the structure or orientation of the region leads to an impairment of the regulation, by nucleotides and fatty acids, of the transport activity. UCP1 is one member of the family formed by the carriers of the mitochondrial inner membrane. The family is characterized by a tripartite structure with three repeated segments of about 100 amino acid residues. Two of the mutations have also been performed in the first and second matrix loops and the effect on UCP1 function is very similar. We conclude that the three matrix loops contribute to the formation of the gating domain in UCP1 and propose that they form a hydrophobic pocket that accommodates the purine moiety of the bound nucleotide. Copyright 1999 Academic Press.
机译：据报道，来自棕色脂肪组织线粒体UCP1的解偶联蛋白区域261-269在控制其质子转运活性中具有重要作用。因此，残基Phe267-Lys268-Gly269的缺失导致蛋白质核苷酸调控的丧失，而区段的完全缺失导致孔的形成。该区域显示出与雌激素受体的DNA结合结构域的序列同源性。本报告通过NMR和圆二色性分析了包含目标残基的20个氨基酸残基肽的结构。我们证明残基263-268采用α螺旋结构。螺旋在第六跨膜结构域的N-末端。已经通过在酵母中重组表达的蛋白质的定点诱变检查了该螺旋的功能重要性。该区域的结构或取向的改变导致核苷酸和脂肪酸对运输活性的调节受损。 UCP1是由线粒体内膜的载体形成的家族成员之一。该家族的特征是具有约100个氨基酸残基的三个重复区段的三方结构。在第一个和第二个矩阵循环中也执行了两个突变，并且它们对UCP1功能的影响非常相似。我们得出的结论是，三个矩阵环有助于UCP1中的门控结构域的形成，并建议它们形成一个疏水性口袋，以容纳结合核苷酸的嘌呤部分。版权所有1999，学术出版社。

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