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5uls

From Proteopedia

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Current revision

Structure of GRP94 in the active conformation

Structural highlights

5uls is a 2 chain structure with sequence from Canis lupus familiaris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.622Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

Publication Abstract from PubMed

Hsp90 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

↑ Huck JD, Que NL, Hong F, Li Z, Gewirth DT. 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. Cell Rep. 2017 Sep 19;20(12):2800-2809. doi: 10.1016/j.celrep.2017.08.079. PMID:28930677 doi:http://dx.doi.org/10.1016/j.celrep.2017.08.079

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5uls"

Categories: Canis lupus familiaris | Large Structures | Gewirth DT | Huck JD | Que NLS

@@ Line 1: / Line 1: @@
 ==Structure of GRP94 in the active conformation==
-<StructureSection load='5uls' size='340' side='right' caption='[[5uls]], [[Resolution|resolution]] 2.62&Aring;' scene=''>
+<StructureSection load='5uls' size='340' side='right'caption='[[5uls]], [[Resolution|resolution]] 2.62&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5uls]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ULS FirstGlance]. <br>
+<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.622&#8491;</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=5uls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uls OCA], [http://pdbe.org/5uls PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uls RCSB], [http://www.ebi.ac.uk/pdbsum/5uls PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uls ProSAT]</span></td></tr>
+<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'>[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>
 == Function ==
-[[http://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).
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Gewirth, D T]]
+[[Category: Canis lupus familiaris]]
-[[Category: Huck, J D]]
+[[Category: Large Structures]]
-[[Category: Que, N L.S]]
+[[Category: Gewirth DT]]
-[[Category: Chaperone]]
+[[Category: Huck JD]]
-[[Category: Endoplasmic reticulum]]
+[[Category: Que NLS]]
-[[Category: Heat-shock protein]]
-[[Category: Hsp90]]

5uls

From Proteopedia

Current revision

Structure of GRP94 in the active conformation

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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