6eob: Difference between revisions
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<StructureSection load='6eob' size='340' side='right' caption='[[6eob]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='6eob' size='340' side='right' caption='[[6eob]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6eob]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EOB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EOB FirstGlance]. <br> | <table><tr><td colspan='2'>[[6eob]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cho_cell_lines Cho cell lines]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EOB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EOB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5o4p|5o4p]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5o4p|5o4p]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">I79_019946 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10029 CHO cell lines])</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=6eob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eob OCA], [http://pdbe.org/6eob PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eob RCSB], [http://www.ebi.ac.uk/pdbsum/6eob PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eob ProSAT]</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=6eob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eob OCA], [http://pdbe.org/6eob PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eob RCSB], [http://www.ebi.ac.uk/pdbsum/6eob PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eob ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Cho cell lines]] | ||
[[Category: Preissler, S]] | |||
[[Category: Read, R J]] | [[Category: Read, R J]] | ||
[[Category: Ron, D]] | [[Category: Ron, D]] | ||
Latest revision as of 13:29, 8 November 2017
Crystal structure of AMPylated GRP78 in apo form (Crystal form 1)Crystal structure of AMPylated GRP78 in apo form (Crystal form 1)
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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