Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters
Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters
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DOI：
10.1016/s0005-2728(02)00343-2
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发表时间：
2002-12-02
影响因子：
4.3
通讯作者：
Hägerhäll, C
中科院分区：
文献类型：
--
作者：
Mathiesen, C;Hägerhäll, C
烟酰胺腺嘌呤二核苷酸还原型（NADH）：醌氧化还原酶（呼吸复合物1）、F420 H2氧化还原酶和复合膜结合的镍铁氢化酶含有与某种类型的真正反向转运蛋白同源的蛋白质亚基。在复合物1中，这些多肽（NuoL/ND 5、NuoM/ND 4、NuoN/ND 2）最有可能是质子泵送机制的核心组分，因此了解更多关于它们的结构和功能是重要的。在这项工作中，我们已经确定了一个这样的多肽的跨膜拓扑结构，并建立了一个2D结构模型的蛋白质有效的所有同源多肽。实验确定的跨膜拓扑结构是不同的预测多数票疏水性分析的超家族成员。一个详细的系统发育分析的一个大的一级序列揭示了这些多肽的功能相关性。(C)2002 Elsevier Science B. V.保留所有权利。
Nicotinamide adenine dinucleotide-reduced form (NADH):quinone oxidoreductase (respiratory Complex 1), F420H2 oxidoreductase and complex, membrane-bound NiFe-hydrogenase contain protein subunits homologous to a certain type of bona fide antiporters. In Complex 1, these polypeptides (NuoL/ND5, NuoM/ND4, NuoN/ND2) are most likely core components of the proton pumping mechanism, and it is thus important to learn more about their structure and function. In this work, we have determined the transmembrane topology of one such polypeptide, and built a 2D structural model of the protein valid for all the homologous polypeptides. The experimentally determined transmembrane topology was different from that predicted by majority vote hydrophobicity analyses of members of the superfamily. A detailed phylogenetic analysis of a large set of primary sequences shed light on the functional relatedness of these polypeptides. (C) 2002 Elsevier Science B.V. All rights reserved.