3qfu

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[[Image:3qfu.png|left|200px]]
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==Crystal structure of Yeast Hsp70 (Bip/kar2) complexed with ADP==
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<StructureSection load='3qfu' size='340' side='right' caption='[[3qfu]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3qfu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QFU FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qfp|3qfp]], [[3qml|3qml]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KAR2, GRP78, SSD1, YJL034W, J1248 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qfu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qfu RCSB], [http://www.ebi.ac.uk/pdbsum/3qfu PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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The line below this paragraph, containing "STRUCTURE_3qfu", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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-->
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{{STRUCTURE_3qfu| PDB=3qfu | SCENE= }}
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===Crystal structure of Yeast Hsp70 (Bip/kar2) complexed with ADP===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_21675960}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 21675960 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_21675960}}
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==About this Structure==
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[[3qfu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QFU OCA].
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==Reference==
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<ref group="xtra">PMID:021675960</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Li, J Z.]]
[[Category: Li, J Z.]]

Revision as of 05:22, 4 June 2014

Crystal structure of Yeast Hsp70 (Bip/kar2) complexed with ADP

3qfu, resolution 1.80Å

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