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2b26

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Revision as of 06:37, 16 May 2018

The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1

Structural highlights

2b26 is a 4 chain structure with sequence from Atcc 18824 and Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	SIS1 (ATCC 18824), Hsc70-2, Hsc2 (DROME)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SIS1_YEAST] Required for nuclear migration during mitosis. It is required for the normal initiation of translation. Might mediate the dissociation of a specific protein complex of the translation machinery. Essential for viability.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Li J, Wu Y, Qian X, Sha B. Crystal structure of yeast Sis1 peptide-binding fragment and Hsp70 Ssa1 C-terminal complex. Biochem J. 2006 Sep 15;398(3):353-60. PMID:16737444 doi:10.1042/BJ20060618

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2b26"

@@ Line 1: / Line 1: @@
 ==The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1==
 <StructureSection load='2b26' size='340' side='right' caption='[[2b26]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2b26]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B26 FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SIS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), Hsc70-2, Hsc2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b26 OCA], [http://pdbe.org/2b26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b26 RCSB], [http://www.ebi.ac.uk/pdbsum/2b26 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b26 OCA], [http://pdbe.org/2b26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b26 RCSB], [http://www.ebi.ac.uk/pdbsum/2b26 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2b26 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b2/2b26_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b2/2b26_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2b26

From Proteopedia

Revision as of 06:37, 16 May 2018

The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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