Cloning, expression, purification and preliminary X-ray crystallographic studies of Escherichia coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1).
Cloning, expression, purification and preliminary X-ray crystallographic studies of Escherichia coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1).
复制标题
大肠杆菌 Hsp100 ClpB 核苷酸结合域 1 (NBD1) 的克隆、表达、纯化和初步 X 射线晶体学研究。
DOI：
10.1107/s0907444901007296
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发表时间：
2001
期刊：
影响因子：
--
通讯作者：
Sha,B
中科院分区：
文献类型：
--
作者：
Li,J;Sha,B
大肠杆菌Hsp100 ClpB在细胞生理学的多伴侣系统中起着关键作用。在被蛋白质或多肽结合激活后，ClpB通过ATP水解性多肽解聚，并允许其他分子伴侣如Hsp70 Dna K和Hsp40 Dna J对非天然多肽进行折叠。ClpB含有两个核苷酸结合域，它们的初级序列中分别含有Walker A和B基序。因此，ClpB可以被归类为与各种细胞活动(AAA)相关的大型ATPase家族的成员。ClpB作为分子伴侣解聚变性多肽的机制尚不清楚。为了研究核苷酸结合结构域如何参与ClpB伴侣活性，我们克隆并结晶了ClpB核苷酸结合结构域1(NBD1)。该晶体利用同步辐射X射线源，衍射率为1.8 ？，属于P212121空间群，晶胞参数为a=38.41，b=65.48，c=79.13 ？MAD方法的结构测定正在进行中。
Escherichia coli Hsp100 ClpB plays critical roles in multi-chaperone systems in cell physiology. After being activated by protein or peptide binding, ClpB disaggregates denatured polypeptides by employing ATP hydrolysis and allows other molecular chaperones such as Hsp70 DnaK and Hsp40 DnaJ to refold the non-native polypeptides. ClpB contains two nucleotide-binding domains with Walker A and B motifs within their primary sequences. Therefore, ClpB can be classified as a member of the large ATPase family known as ATPases associated with various cellular activities (AAAs). The mechanisms by which the ClpB acts as a molecular chaperone to disaggregate denatured polypeptides are unknown. To investigate how the nucleotide-binding domain participates in ClpB chaperone activity, we have cloned and crystallized ClpB nucleotide-binding domain 1 (NBD1). The ClpB NBD1 crystals diffract to 1.80 Å using a synchrotron X-ray source and belong to the space group P212121, with unit-cell parameters a = 38.41, b = 65.48, c = 79.13 Å. Structure determination by the MAD method is under way.
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