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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The N-terminal substrate-recognition domain of a LonC protease exhibits structural and functional similarity to cytosolic chaperones
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The N-terminal substrate-recognition domain of a LonC protease exhibits structural and functional similarity to cytosolic chaperones

机译：氨基substrate-recognition域的LonC蛋白酶展品结构和功能相似胞质陪伴

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摘要

The Lon protease is ubiquitous in nature. Its proteolytic activity is associated with diverse cellular functions ranging from maintaining proteostasis under normal and stress conditions to regulating cell metabolism. Although Lon was originally identified as an ATP-dependent protease with fused AAA+ (ATPases associated with diverse cellular activities) and protease domains, analyses have recently identified LonC as a class of Lon-like proteases with no intrinsic ATPase activity. In contrast to the canonical ATP-dependent Lon present in eukaryotic organelles and prokaryotes, LonC contains an AAA-like domain that lacks the conserved ATPase motifs. Moreover, the LonC AAA-like domain is inserted with a large domain predicted to be largely -helical; intriguingly, this unique Lon-insertion domain (LID) was disordered in the recently determined full-length crystal structure of Meiothermus taiwanensis LonC (MtaLonC). Here, the crystal structure of the N-terminal AAA-like /β subdomain of MtaLonC containing an intact LID, which forms a large -helical hairpin protruding from the AAA-like domain, is reported. The structure of the LID is remarkably similar to the tentacle-like prong of the periplasmic chaperone Skp. It is shown that the LID of LonC is involved both in Skp-like chaperone activity and in recognition of unfolded protein substrates. The structure allows the construction of a complete model of LonC with six helical hairpin extensions defining a basket-like structure atop the AAA ring and encircling the entry portal to the barrel-like degradation chamber of Lon.
机译：朗蛋白酶在本质上是无处不在的。蛋白水解活性与多样化从维持细胞功能proteostasis在正常和压力条件调节细胞新陈代谢。最初作为一个ATP-dependent识别蛋白酶与融合AAA + (atp酶有关不同的细胞活动)和蛋白酶域,分析最近LonC识别作为一类Lon-like蛋白酶没有内在的atp酶活性。规范ATP-dependent朗在真核生物细胞器和原核生物,LonC包含一个AAA-like领域缺乏守恒的腺苷三磷酸酶图案。插入与一个大域预测很大程度上螺旋;Lon-insertion域(盖子)是无序的最近确定完整的晶体结构的Meiothermus taiwanensis LonC (MtaLonC)。氨基端AAA-like的晶体结构/β子域名MtaLonC包含一个完整的盖子,形成一个大型螺旋发卡突出从AAA-like域,报道。盖子的结构非常相似周质的伴侣的触角耙子Skp。无论是在Skp-like伴侣和活动识别的蛋白质基质。结构允许一个完整的建设工作模型LonC六螺旋发卡扩展定义一个像篮子般的结构在AAA环和包围的入口门户barrel-like退化的经度。

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