5uls: Difference between revisions
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<StructureSection load='5uls' size='340' side='right'caption='[[5uls]], [[Resolution|resolution]] 2.62Å' scene=''> | <StructureSection load='5uls' size='340' side='right'caption='[[5uls]], [[Resolution|resolution]] 2.62Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5uls]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5uls]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ULS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ULS FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.622Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5uls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uls OCA], [https://pdbe.org/5uls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uls RCSB], [https://www.ebi.ac.uk/pdbsum/5uls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uls ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ENPL_CANLF ENPL_CANLF] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Canis lupus familiaris]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gewirth | [[Category: Gewirth DT]] | ||
[[Category: Huck | [[Category: Huck JD]] | ||
[[Category: Que | [[Category: Que NLS]] | ||
Latest revision as of 16:29, 4 October 2023
Structure of GRP94 in the active conformationStructure of GRP94 in the active conformation
Structural highlights
FunctionENPL_CANLF Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity). Publication Abstract from PubMedHsp90 chaperones undergo ATP-driven conformational changes during the maturation of client proteins, populating a closed state upon ATP binding in which the N-terminal domains of the homodimer form a second inter-protomer dimer interface. A structure of GRP94, the endoplasmic reticulum hsp90, in a closed conformation has not been described, and the determinants that regulate closure are not well understood. Here, we determined the 2.6-A structure of AMPPNP-bound GRP94 in the closed dimer conformation. The structure includes the pre-N domain, a region preceding the N-terminal domain that is highly conserved in GRP94, but not in other hsp90s. We show that the GRP94 pre-N domain is essential for client maturation, and we identify the pre-N domain as an important regulator of ATPase rates and dimer closure. The structure also reveals a GRP94:polypeptide interaction that partially mimics a client-bound state. The results provide structural insight into the ATP-dependent client maturation process of GRP94. Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site.,Huck JD, Que NL, Hong F, Li Z, Gewirth DT Cell Rep. 2017 Sep 19;20(12):2800-2809. doi: 10.1016/j.celrep.2017.08.079. PMID:28930677[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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