The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40.
The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40.
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DOI：
10.1016/j.jmb.2004.12.040
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发表时间：
2005-03
影响因子：
5.6
通讯作者：
Yunkun Wu;Jingzhi Li;Zhongmin Jin;Zhengqing Fu;B. Sha
中科院分区：
文献类型：
--
作者：
Yunkun Wu;Jingzhi Li;Zhongmin Jin;Zhengqing Fu;B. Sha
分子伴侣Hsp40作为二聚体起作用。二聚体的形成对Hsp40分子伴侣活性至关重要，以促进Hsp70对非天然多肽的再折叠。我们用MAD方法确定了酵母Hsp40 Ydj1的c端片段的晶体结构，该片段与Ydj1二聚化有关。Ydj1的c端片段由Ydj1的结构域III和Ydj1 c端二聚基序组成。晶体结构表明，I型Hsp40 Ydj1的二聚化基序与酵母II型Hsp40的二聚化基序有显著差异。在同型二聚体中，来自一个单体的I型Hsp40 Ydj1的C端与来自另一个单体的结构域III形成β-链。来自ydj1c末端的L372将其侧链插入到III结构域的疏水口袋中。模拟的Ydj1全长二聚体结构表明，两个单体之间形成了较大的间隙。含有锌指基序的Ydj1单体的结构域ii直接相互指向。
The molecular chaperone Hsp40 functions as a dimer. The dimer formation is critical for Hsp40 molecular chaperone activity to facilitate Hsp70 to refold non-native polypeptides. We have determined the crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 that is responsible for Ydj1 dimerization by MAD method. The C-terminal fragment of Ydj1 comprises of the domain III of Ydj1 and the Ydj1 C-terminal dimerization motif. The crystal structure indicates that the dimerization motif of type I Hsp40 Ydj1 differs significantly from that of yeast type II Hsp40. The C terminus of type I Hsp40 Ydj1 from one monomer forms β-strands with the domain III from the other monomer in the homo-dimer. The L372 from Ydj1 C terminus inserts its side-chain into a hydrophobic pocket on domain III. The modeled full-length Ydj1 dimer structure reveals that a large cleft is formed between the two monomers. The domain IIs of Ydj1 monomers that contain the zinc-finger motifs points directly against each other.