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==Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP== | |||
<StructureSection load='4jne' size='340' side='right' caption='[[4jne]], [[Resolution|resolution]] 1.96Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4jne]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JNE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JNE FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jn4|4jn4]], [[4jnf|4jnf]]</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=4jne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jne OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jne RCSB], [http://www.ebi.ac.uk/pdbsum/4jne PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 70-kilodalton (kDa) heat-shock proteins (Hsp70s) are ubiquitous molecular chaperones essential for cellular protein folding and proteostasis. Each Hsp70 has two functional domains: a nucleotide-binding domain (NBD), which binds and hydrolyzes ATP, and a substrate-binding domain (SBD), which binds extended polypeptides. NBD and SBD interact little when in the presence of ADP; however, ATP binding allosterically couples the polypeptide- and ATP-binding sites. ATP binding promotes polypeptide release; polypeptide rebinding stimulates ATP hydrolysis. This allosteric coupling is poorly understood. Here we present the crystal structure of an intact ATP-bound Hsp70 from Escherichia coli at 1.96-A resolution. The ATP-bound NBD adopts a unique conformation, forming extensive interfaces with an SBD that has changed radically, having its alpha-helical lid displaced and the polypeptide-binding channel of its beta-subdomain restructured. These conformational changes, together with our biochemical assays, provide a structural explanation for allosteric coupling in Hsp70 activity. | |||
Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP.,Qi R, Sarbeng EB, Liu Q, Le KQ, Xu X, Xu H, Yang J, Wong JL, Vorvis C, Hendrickson WA, Zhou L, Liu Q Nat Struct Mol Biol. 2013 Jul;20(7):900-7. doi: 10.1038/nsmb.2583. Epub 2013 May , 26. PMID:23708608<ref>PMID:23708608</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
[[Category: Hendrickson, W A | [[Category: Hendrickson, W A]] | ||
[[Category: Le, K Q | [[Category: Le, K Q]] | ||
[[Category: Liu, Q | [[Category: Liu, Q]] | ||
[[Category: Qi, R | [[Category: Qi, R]] | ||
[[Category: Sarbeng, E B | [[Category: Sarbeng, E B]] | ||
[[Category: Vorvis, C | [[Category: Vorvis, C]] | ||
[[Category: Wong, J L | [[Category: Wong, J L]] | ||
[[Category: Xu, H | [[Category: Xu, H]] | ||
[[Category: Xu, X | [[Category: Xu, X]] | ||
[[Category: Yang, J | [[Category: Yang, J]] | ||
[[Category: Zhou, L | [[Category: Zhou, L]] | ||
[[Category: Allosteric coupling]] | [[Category: Allosteric coupling]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Dnak]] | [[Category: Dnak]] | ||
Revision as of 18:20, 21 December 2014
Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATPAllosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
Structural highlights
Publication Abstract from PubMedThe 70-kilodalton (kDa) heat-shock proteins (Hsp70s) are ubiquitous molecular chaperones essential for cellular protein folding and proteostasis. Each Hsp70 has two functional domains: a nucleotide-binding domain (NBD), which binds and hydrolyzes ATP, and a substrate-binding domain (SBD), which binds extended polypeptides. NBD and SBD interact little when in the presence of ADP; however, ATP binding allosterically couples the polypeptide- and ATP-binding sites. ATP binding promotes polypeptide release; polypeptide rebinding stimulates ATP hydrolysis. This allosteric coupling is poorly understood. Here we present the crystal structure of an intact ATP-bound Hsp70 from Escherichia coli at 1.96-A resolution. The ATP-bound NBD adopts a unique conformation, forming extensive interfaces with an SBD that has changed radically, having its alpha-helical lid displaced and the polypeptide-binding channel of its beta-subdomain restructured. These conformational changes, together with our biochemical assays, provide a structural explanation for allosteric coupling in Hsp70 activity. Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP.,Qi R, Sarbeng EB, Liu Q, Le KQ, Xu X, Xu H, Yang J, Wong JL, Vorvis C, Hendrickson WA, Zhou L, Liu Q Nat Struct Mol Biol. 2013 Jul;20(7):900-7. doi: 10.1038/nsmb.2583. Epub 2013 May , 26. PMID:23708608[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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