2b26: Difference between revisions

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[[Image:2b26.jpg|left|200px]]<br /><applet load="2b26" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2b26.jpg|left|200px]]<br /><applet load="2b26" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2b26, resolution 3.2Å" />

'''The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2B26 OCA].

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==

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[[Category: hsp40 sis1 hsp70 ssa1]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 08:31:~~50 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:33:26 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2b26.jpg|left|200px]]<br /><applet load="2b26" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2b26.jpg|left|200px]]<br /><applet load="2b26" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2b26, resolution 3.2&Aring;" />
 '''The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1'''<br />
 ==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.
+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==
-B26 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B26 OCA].
+B26 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==
@@ Line 20: / Line 20: @@
 [[Category: hsp40 sis1 hsp70 ssa1]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:31:50 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:33:26 2008''