5vca: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5vca is ~~ON HOLD~~

==VCP like ATPase from T. acidophilum (VAT)-Substrate bound conformation==

== Structural highlights ==

<table><tr><td colspan='2'>[[5vca]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VCA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VCA FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vc7|5vc7]]</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=5vca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vca OCA], [http://pdbe.org/5vca PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vca RCSB], [http://www.ebi.ac.uk/pdbsum/5vca PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vca ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

AAA+ unfoldases are thought to unfold substrate through the central pore of their hexameric structures, but how this process occurs is not known. VAT, the Thermoplasma acidophilum homologue of eukaryotic CDC48/p97, works in conjunction with the proteasome to degrade misfolded or damaged proteins. We show that in the presence of ATP, VAT with its regulatory N-terminal domains removed unfolds other VAT complexes as substrate. We captured images of this transient process by electron cryomicroscopy (cryo-EM) to reveal the structure of the substrate-bound intermediate. Substrate binding breaks the six-fold symmetry of the complex, allowing five of the six VAT subunits to constrict into a tight helix that grips an ~80 A stretch of unfolded protein. The structure suggests a processive hand-over-hand unfolding mechanism, where each VAT subunit releases the substrate in turn before re-engaging further along the target protein, thereby unfolding it.

~~Authors~~:

Structure of a AAA+ unfoldase in the process of unfolding substrate.,Ripstein ZA, Huang R, Augustyniak R, Kay LE, Rubinstein JL Elife. 2017 Apr 8;6. pii: e25754. doi: 10.7554/eLife.25754. PMID:28390173<ref>PMID:28390173</ref>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Augustyniak, R]]

[[Category: Huang, R]]

[[Category: Kay, L E]]

[[Category: Ripstein, Z A]]

[[Category: Rubinstein, J L]]

[[Category: Aaa+]]

[[Category: Atpase]]

[[Category: Complex]]

[[Category: Hydrolase]]

[[Category: Unfoldase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5vca is ON HOLD
+==VCP like ATPase from T. acidophilum (VAT)-Substrate bound conformation==
+<StructureSection load='5vca' size='340' side='right' caption='[[5vca]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5vca]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VCA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VCA FirstGlance]. <br>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vc7|5vc7]]</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=5vca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vca OCA], [http://pdbe.org/5vca PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vca RCSB], [http://www.ebi.ac.uk/pdbsum/5vca PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vca ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+AAA+ unfoldases are thought to unfold substrate through the central pore of their hexameric structures, but how this process occurs is not known. VAT, the Thermoplasma acidophilum homologue of eukaryotic CDC48/p97, works in conjunction with the proteasome to degrade misfolded or damaged proteins. We show that in the presence of ATP, VAT with its regulatory N-terminal domains removed unfolds other VAT complexes as substrate. We captured images of this transient process by electron cryomicroscopy (cryo-EM) to reveal the structure of the substrate-bound intermediate. Substrate binding breaks the six-fold symmetry of the complex, allowing five of the six VAT subunits to constrict into a tight helix that grips an ~80 A stretch of unfolded protein. The structure suggests a processive hand-over-hand unfolding mechanism, where each VAT subunit releases the substrate in turn before re-engaging further along the target protein, thereby unfolding it.
-Authors:
+Structure of a AAA+ unfoldase in the process of unfolding substrate.,Ripstein ZA, Huang R, Augustyniak R, Kay LE, Rubinstein JL Elife. 2017 Apr 8;6. pii: e25754. doi: 10.7554/eLife.25754. PMID:28390173<ref>PMID:28390173</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5vca" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Augustyniak, R]]
+[[Category: Huang, R]]
+[[Category: Kay, L E]]
+[[Category: Ripstein, Z A]]
+[[Category: Rubinstein, J L]]
+[[Category: Aaa+]]
+[[Category: Atpase]]
+[[Category: Complex]]
+[[Category: Hydrolase]]
+[[Category: Unfoldase]]