The PRC-barrel: a widespread, conserved domain shared by photosynthetic reaction center subunits and proteins of RNA metabolism.
The PRC-barrel: a widespread, conserved domain shared by photosynthetic reaction center subunits and proteins of RNA metabolism.
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DOI：
10.1186/gb-2002-3-11-research0061
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发表时间：
2002-10-14
期刊：
影响因子：
12.3
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中科院分区：
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PRC-H β-桶结构域是一种独特的细胞质 β-桶结构域，其折叠与任何其他众所周知的 β-桶结构域没有密切的结构关系，是大约 80 个残基长的新型蛋白质结构域超家族的原型。这个领域是一个广泛存在的古老领域，似乎已被招募到各种生物系统中，从 RNA 处理到光合作用。紫色细菌光合反应中心（PRC-H）的H亚基对于光合反应中心的组装很重要，并且似乎在仲醌还原过程中调节电子转移。它包含一个独特的细胞质 β-桶结构域，其折叠与任何其他众所周知的 β-桶结构域没有密切的结构关系。我们表明，PRC-H β-桶结构域是新型蛋白质结构域超家族（PRC-桶）的原型，大约有 80 个残基长，广泛存在于细菌、古细菌和植物中。该结构域也存在于泛细菌蛋白 RimM 的羧基末端，该蛋白参与核糖体成熟和 16S rRNA 的加工。所有已知广古菌中保守的小蛋白家族完全由该结构域的单个独立副本组成。来自光合变形菌的该结构域的版本包含保守的酸性残基，被认为可以调节光诱导的电子转移反应中醌的还原。含有这种酸性残基的密切相关形式也存在于几种非光合细菌以及蓝细菌中，它们具有不同组织的反应中心。我们还表明该结构域包含几个可以介导特定蛋白质-蛋白质相互作用的决定因素。 PRC-barrel 是一个广泛存在的古老领域，似乎已被招募到从 RNA 处理到光合作用的各种生物系统中。鉴定众多蛋白质中的这种多功能结构域可以帮助研究其生物学中未探索的方面。
The PRC-H β-barrel domain, a distinct cytoplasmic β-barrel domain whose fold has no close structural relationship to any other well known β-barrel domain, is the prototype of a novel superfamily of protein domains approximately 80 residues long. This domian is a widespread, ancient domain that appears to have been recruited to a variety of biological systems, ranging from RNA processing to photosynthesis. The H subunit of the purple bacterial photosynthetic reaction center (PRC-H) is important for the assembly of the photosynthetic reaction center and appears to regulate electron transfer during the reduction of the secondary quinone. It contains a distinct cytoplasmic β-barrel domain whose fold has no close structural relationship to any other well known β-barrel domain. We show that the PRC-H β-barrel domain is the prototype of a novel superfamily of protein domains, the PRC-barrels, approximately 80 residues long, which is widely represented in bacteria, archaea and plants. This domain is also present at the carboxyl terminus of the pan-bacterial protein RimM, which is involved in ribosomal maturation and processing of 16S rRNA. A family of small proteins conserved in all known euryarchaea are composed entirely of a single stand-alone copy of the domain. Versions of this domain from photosynthetic proteobacteria contain a conserved acidic residue that is thought to regulate the reduction of quinones in the light-induced electron-transfer reaction. Closely related forms containing this acidic residue are also found in several non-photosynthetic bacteria, as well as in cyanobacteria, which have reaction centers with a different organization. We also show that the domain contains several determinants that could mediate specific protein-protein interactions. The PRC-barrel is a widespread, ancient domain that appears to have been recruited to a variety of biological systems, ranging from RNA processing to photosynthesis. Identification of this versatile domain in numerous proteins could aid investigation of unexplored aspects of their biology.