3qfp: Difference between revisions

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<StructureSection load='3qfp' size='340' side='right'caption='[[3qfp]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
<StructureSection load='3qfp' size='340' side='right'caption='[[3qfp]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3qfp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QFP FirstGlance]. <br>
<table><tr><td colspan='2'>[[3qfp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QFP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qfu|3qfu]], [[3qml|3qml]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KAR2, GRP78, SSD1, YJL034W, J1248 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qfp OCA], [https://pdbe.org/3qfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qfp RCSB], [https://www.ebi.ac.uk/pdbsum/3qfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qfp ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qfp OCA], [https://pdbe.org/3qfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qfp RCSB], [https://www.ebi.ac.uk/pdbsum/3qfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qfp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/GRP78_YEAST GRP78_YEAST]] Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.<ref>PMID:16002399</ref> 
[https://www.uniprot.org/uniprot/BIP_YEAST BIP_YEAST] Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.<ref>PMID:16002399</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sil1 functions as a nucleotide exchange factor (NEF) for Bip in eukaryotic cells. In order to understand how Sil1 functions as a NEF, we analyzed the crystal structure of the yeast Bip-Sil1 complex at a resolution of 2.3A. In the complex, the Sil1 molecule acts as a "molecular clamp" which binds to the IIb lobe of the Bip ATPase domain. Sil1 binding causes lobe IIb to rotate ~13.5 degrees away from the ADP-binding pocket and lobe Ib to rotate in the opposite direction for ~3.7 degrees . These conformational changes in Bip open up the nucleotide-binding pocket in the ATPase domain and simultaneously disrupt the hydrogen bonds between Bip and bound ADP, thus providing a mechanism for ADP release. We also demonstrate that Sil1 mutations that disrupt binding to the Bip ATPase domain abolish Sil1's ability to stimulate Bip ATPase activity.
 
Structural analysis of the Sil1-Bip complex reveals how Sil1 functions as a nucleotide exchange factor.,Yan M, Li J, Sha B Biochem J. 2011 Jun 15. PMID:21675960<ref>PMID:21675960</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qfp" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Li, J Z]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Sha, B D]]
[[Category: Li JZ]]
[[Category: Yan, M]]
[[Category: Sha BD]]
[[Category: Chaperone]]
[[Category: Yan M]]
[[Category: Hsp70]]

Latest revision as of 11:43, 14 March 2024

Crystal structure of yeast Hsp70 (Bip/Kar2) ATPase domain

3qfp, resolution 2.26Å

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