2b26: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2b26.jpg|left|200px]] | [[Image:2b26.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_2b26", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_2b26| PDB=2b26 | SCENE= }} | |||
| | |||
| | |||
}} | |||
'''The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1''' | '''The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1''' | ||
| Line 30: | Line 27: | ||
[[Category: Sha, B.]] | [[Category: Sha, B.]] | ||
[[Category: Wu, Y.]] | [[Category: Wu, Y.]] | ||
[[Category: | [[Category: Hsp40 sis1 hsp70 ssa1]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:45:36 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 19:45, 3 May 2008
The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1
OverviewOverview
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 StructureAbout this Structure
2B26 is a Protein complex structure of sequences from Drosophila melanogaster and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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 Sat May 3 19:45:36 2008