1c3g: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1c3g.gif|left|200px]]
{{Seed}}
[[Image:1c3g.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1c3g|  PDB=1c3g  |  SCENE=  }}  
{{STRUCTURE_1c3g|  PDB=1c3g  |  SCENE=  }}  


'''S. CEREVISIAE HEAT SHOCK PROTEIN 40 SIS1'''
===S. CEREVISIAE HEAT SHOCK PROTEIN 40 SIS1===




==Overview==
<!--
BACKGROUND: Molecular chaperone Hsp40 can bind non-native polypeptide and facilitate Hsp70 in protein refolding. How Hsp40 and other chaperones distinguish between the folded and unfolded states of proteins to bind nonnative polypeptides is a fundamental issue. RESULTS: To investigate this mechanism, we determined the crystal structure of the peptide-binding fragment of Sis1, an essential member of the Hsp40 family from Saccharomyces cerevisiae. The 2.7 A structure reveals that Sis1 forms a homodimer in the crystal by a crystallographic twofold axis. Sis1 monomers are elongated and consist of two domains with similar folds. Sis1 dimerizes through a short C-terminal stretch. The Sis1 dimer has a U-shaped architecture and a large cleft is formed between the two elongated monomers. Domain I in each monomer contains a hydrophobic depression that might be involved in binding the sidechains of hydrophobic amino acids. CONCLUSIONS: Sis1 (1-337), which lacks the dimerization motif, exhibited severe defects in chaperone activity, but could regulate Hsp70 ATPase activity. Thus, dimer formation is critical for Sis1 chaperone function. We propose that the Sis1 cleft functions as a docking site for the Hsp70 peptide-binding domain and that Sis1-Hsp70 interaction serves to facilitate the efficient transfer of peptides from Sis1 to Hsp70.
The line below this paragraph, {{ABSTRACT_PUBMED_10997899}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10997899 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10997899}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Beta sheet]]
[[Category: Beta sheet]]
[[Category: Short helice]]
[[Category: Short helice]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:16:54 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:09:17 2008''

Revision as of 17:09, 30 June 2008

File:1c3g.png

Template:STRUCTURE 1c3g

S. CEREVISIAE HEAT SHOCK PROTEIN 40 SIS1

Template:ABSTRACT PUBMED 10997899

About this Structure

1C3G is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1., Sha B, Lee S, Cyr DM, Structure. 2000 Aug 15;8(8):799-807. PMID:10997899

Page seeded by OCA on Mon Jun 30 20:09:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1c3g&oldid=580813"