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嗜热栖热袍菌NA1中Lon蛋白的结晶及初步X射线晶体学分析。

Crystallization and preliminary X-ray crystallographic analysis of Lon from Thermococcus onnurineus NA1.

作者信息

An Young Jun, Lee Chang-Ro, Supangat Supangat, Lee Hyun Sook, Lee Jung-Hyun, Kang Sung Gyun, Cha Sun-Shin

机构信息

Marine Biotechnology Research Center, Korea Ocean Research and Development Institute, Ansan 426-744, Republic of Korea.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):54-6. doi: 10.1107/S1744309109048039. Epub 2009 Dec 25.

DOI:10.1107/S1744309109048039
PMID:20057071
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2805537/
Abstract

Lon is an oligomeric ATP-dependent protease that degrades defective or denatured proteins as well as some folded proteins for the control of cellular protein quality and metabolism. Lon from Thermococcus onnurineus NA1 was purified and crystallized at 295 K. A 2.0 A resolution data set was collected using synchrotron radiation. The crystals belonged to space group P6(3), with unit-cell parameters a = 121.45, b = 121.45, c = 195.24 A. Assuming the presence of two monomers in the asymmetric unit, the solvent content was estimated to be about 60.7%.

摘要

Lon是一种寡聚的ATP依赖性蛋白酶，它可降解有缺陷或变性的蛋白质以及一些折叠蛋白，以控制细胞蛋白质质量和代谢。从嗜热栖热袍菌NA1中纯化得到的Lon在295 K下结晶。使用同步辐射收集了分辨率为2.0 Å的数据集。晶体属于空间群P6(3)，晶胞参数a = 121.45，b = 121.45，c = 195.24 Å。假设不对称单元中存在两个单体，溶剂含量估计约为60.7%。

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The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism.嗜热栖热球菌NA1的全基因组序列揭示了一种混合的异养和一氧化碳营养代谢方式。
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Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains.剖析一种蛋白酶：从对分离结构域的研究中获得的ATP依赖型Lon蛋白酶的结构特征
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