2b26
From Proteopedia
(New page: 200px<br /><applet load="2b26" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b26, resolution 3.2Å" /> '''The crystal structure...) |
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| - | [[Image:2b26.jpg|left|200px]]<br /><applet load="2b26" size=" | + | [[Image:2b26.jpg|left|200px]]<br /><applet load="2b26" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2b26, resolution 3.2Å" /> | caption="2b26, resolution 3.2Å" /> | ||
'''The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1'''<br /> | '''The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Heat shock protein (Hsp) 40 facilitates the critical role of Hsp70 in a | + | Heat shock protein (Hsp) 40 facilitates the critical role of Hsp70 in a number of cellular processes such as protein folding, assembly, degradation and translocation in vivo. Hsp40 and Hsp70 stay in close contact to achieve these diverse functions. The conserved C-terminal EEVD motif in Hsp70 has been shown to regulate Hsp40-Hsp70 interaction by an unknown mechanism. Here, we provide a structural basis for this regulation by determining the crystal structure of yeast Hsp40 Sis1 peptide-binding fragment complexed with the Hsp70 Ssa1 C-terminal. The Ssa1 extreme C-terminal eight residues, G634PTVEEVD641, form a beta-strand with the domain I of Sis1 peptide-binding fragment. Surprisingly, the Ssa1 C-terminal binds Sis1 at the site where Sis1 interacts with the non-native polypeptides. The negatively charged residues within the EEVD motif in Ssa1 C-terminal form extensive charge-charge interactions with the positively charged residues in Sis1. The structure-based mutagenesis data support the structural observations. |
==About this Structure== | ==About this Structure== | ||
| - | 2B26 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 2B26 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B26 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hsp40 sis1 hsp70 ssa1]] | [[Category: hsp40 sis1 hsp70 ssa1]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:33:26 2008'' |
Revision as of 14:33, 21 February 2008
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The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1
Overview
Heat shock protein (Hsp) 40 facilitates the critical role of Hsp70 in a number of cellular processes such as protein folding, assembly, degradation and translocation in vivo. Hsp40 and Hsp70 stay in close contact to achieve these diverse functions. The conserved C-terminal EEVD motif in Hsp70 has been shown to regulate Hsp40-Hsp70 interaction by an unknown mechanism. Here, we provide a structural basis for this regulation by determining the crystal structure of yeast Hsp40 Sis1 peptide-binding fragment complexed with the Hsp70 Ssa1 C-terminal. The Ssa1 extreme C-terminal eight residues, G634PTVEEVD641, form a beta-strand with the domain I of Sis1 peptide-binding fragment. Surprisingly, the Ssa1 C-terminal binds Sis1 at the site where Sis1 interacts with the non-native polypeptides. The negatively charged residues within the EEVD motif in Ssa1 C-terminal form extensive charge-charge interactions with the positively charged residues in Sis1. The structure-based mutagenesis data support the structural observations.
About this Structure
2B26 is a Protein complex structure of sequences from Drosophila melanogaster and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of yeast Sis1 peptide-binding fragment and Hsp70 Ssa1 C-terminal complex., Li J, Wu Y, Qian X, Sha B, Biochem J. 2006 Sep 15;398(3):353-60. PMID:16737444
Page seeded by OCA on Thu Feb 21 16:33:26 2008
