6eoc - Revision history

OCA at 12:46, 7 November 2018

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OCA: Protected "6eoc" [edit=sysop:move=sysop]

OCA — Wed, 01 Nov 2017 06:13:24 GMT

Protected "6eoc" [edit=sysop:move=sysop]

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Revision as of 06:13, 1 November 2017

OCA: New page: ==Crystal structure of AMPylated GRP78 in apo form (Crystal form 2)==
OCA — Wed, 01 Nov 2017 06:13:23 GMT

New page: ==Crystal structure of AMPylated GRP78 in apo form (Crystal form 2)== <StructureSection load='6eoc' size='340' side='right' caption='6eoc, resolution 1.67Å' scene...

New page

==Crystal structure of AMPylated GRP78 in apo form (Crystal form 2)==
<StructureSection load='6eoc' size='340' side='right' caption='[[6eoc]], [[Resolution|resolution]] 1.67Å' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6eoc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EOC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EOC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</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">[[5o4p|5o4p]]</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=6eoc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eoc OCA], [http://pdbe.org/6eoc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eoc RCSB], [http://www.ebi.ac.uk/pdbsum/6eoc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eoc ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The endoplasmic reticulum (ER)-localized Hsp70 chaperone BiP contributes to protein folding homeostasis by engaging unfolded client proteins in a process that is tightly coupled to ATP binding and hydrolysis. The inverse correlation between AMPylation and the burden of unfolded ER proteins suggests a post-translational mechanism for adjusting BiP's activity to changing levels of ER stress, but the underlying molecular details are unexplored. We present biochemical and crystallographic studies indicating that irrespective of the identity of the bound nucleotide AMPylation biases BiP towards a conformation normally attained by the ATP-bound chaperone. AMPylation does not affect the interaction between BiP and J-protein co-factors but appears to allosterically impair J protein-stimulated ATP-hydrolysis, resulting in the inability of modified BiP to attain high affinity for its substrates. These findings suggest a molecular mechanism by which AMPylation serves as a switch to inactivate BiP, limiting its interactions with substrates whilst conserving ATP.

AMPylation targets the rate-limiting step of BiP's ATPase cycle for its functional inactivation.,Preissler S, Rohland L, Yan Y, Chen R, Read RJ, Ron D Elife. 2017 Oct 24;6. pii: e29428. doi: 10.7554/eLife.29428. PMID:29064368<ref>PMID:29064368</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6eoc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
TOC
</StructureSection>
[[Category: Preissler, S]]
[[Category: Read, R J]]
[[Category: Ron, D]]
[[Category: Yan, Y]]
[[Category: Ampylation]]
[[Category: Apo]]
[[Category: Bip]]
[[Category: Chaperone]]
[[Category: Grp78]]