Recent developments in nucleobase cation symporter-1 (NCS1) family transport proteins from bacteria, archaea, fungi and plants

Recent developments in nucleobase cation symporter-1 (NCS1) family transport proteins from bacteria, archaea, fungi and plants
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核碱基阳离子同向转运蛋白 1 (NCS1) 家族转运细菌、古细菌、真菌和植物蛋白的最新进展

DOI:
10.1007/s12038-018-9780-3
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发表时间:
2018
影响因子:
2.9
通讯作者:
Patching S
Patching S
中科院分区:
生物学4区
文献类型:
--
作者:
Patching S

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核碱基阳离子同向转运体-I(NCS 1)家族的次级活性转运蛋白包括来自细菌、古细菌、真菌和植物的超过2500个测序成员。NCS 1蛋白使用质子或钠梯度来驱动嘌呤和嘧啶核碱基和核苷、乙内酰脲和相关化合物的向内细胞转运。NCS 1蛋白质的结构组织、底物结合残基和分子机制由钠偶联乙内酰脲转运蛋白Mhp 1的晶体结构定义。植物蛋白与细菌/古细菌蛋白以及不同的Fur型和Fc y型真菌蛋白和植物蛋白最密切相关,这些蛋白通过独立的水平转移从原核生物起源。对25种实验表征的蛋白质的分析揭示了细菌蛋白质中的高底物特异性、Fur型和Fc y型真菌蛋白质中的不同非重叠特异性以及植物蛋白质中的广泛特异性。可能的结构解释是确定细菌蛋白质之间的底物特异性的差异,而其他蛋白质的特异性不能通过简单的序列比较来预测。特异性似乎具有种属特异性,并由主要底物结合位点和门控结构域中多个残基决定的效应组合决定。本文就NCS 1蛋白的进化关系、功能和结构组织、底物特异性的分子机制和起源以及未来的研究方向作一综述。
The nucleobase cation symporter-1 (NCS1) family of secondary active transport proteins comprises over 2500 sequenced members from bacteria, archaea, fungi and plants. NCS1 proteins use a proton or sodium gradient to drive inward cellular transport of purine and pyrimidine nucleobases and nucleosides, hydantoins and related compounds. The structural organization, substrate binding residues and molecular mechanism of NCS1 proteins are defined by crystal structures of sodium-coupled hydantoin transporter, Mhp1. Plant proteins are most closely related to bacterial/archaeal proteins and the distinct Fur-type and Fcy-type fungal proteins and plant proteins originated through independent horizontal transfers from prokaryotes. Analyses of 25 experimentally characterized proteins reveal high substrate specificity in bacterial proteins, distinct non-overlapping specificities in Fur-type and Fcy-type fungal proteins and broad specificity in plant proteins. Possible structural explanations are identified for differences in substrate specificity between bacterial proteins, whilst specificities of other proteins cannot be predicted by simple sequence comparisons. Specificity appears to be species specific and determined by combinations of effects dictated by multiple residues in the major substrate binding site and gating domains. This is an exploratory research review of evolutionary relationships, function and structural organization, molecular mechanism and origins of substrate specificity in NCS1 proteins and avenues of future direction.
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