2o1t

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (00:13, 28 December 2023) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2o1t.png|left|200px]]
 
-
{{STRUCTURE_2o1t| PDB=2o1t | SCENE= }}
+
==Structure of Middle plus C-terminal domains (M+C) of GRP94==
 +
<StructureSection load='2o1t' size='340' side='right'caption='[[2o1t]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2o1t]] is a 10 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=2O1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O1T FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</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=2o1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o1t OCA], [https://pdbe.org/2o1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o1t RCSB], [https://www.ebi.ac.uk/pdbsum/2o1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o1t ProSAT]</span></td></tr>
 +
</table>
 +
== 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).
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o1/2o1t_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2o1t ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
GRP94, an essential endoplasmic reticulum chaperone, is required for the conformational maturation of proteins destined for cell-surface display or export. The extent to which GRP94 and its cytosolic paralog, Hsp90, share a common mechanism remains controversial. GRP94 has not been shown conclusively to hydrolyze ATP or bind cochaperones, and both activities, by contrast, result in conformational changes and N-terminal dimerization in Hsp90 that are critical for its function. Here, we report the 2.4 A crystal structure of mammalian GRP94 in complex with AMPPNP and ADP. The chaperone is conformationally insensitive to the identity of the bound nucleotide, adopting a "twisted V" conformation that precludes N-terminal domain dimerization. We also present conclusive evidence that GRP94 possesses ATPase activity. Our observations provide a structural explanation for GRP94's observed rate of ATP hydrolysis and suggest a model for the role of ATP binding and hydrolysis in the GRP94 chaperone cycle.
-
===Structure of Middle plus C-terminal domains (M+C) of GRP94===
+
Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones.,Dollins DE, Warren JJ, Immormino RM, Gewirth DT Mol Cell. 2007 Oct 12;28(1):41-56. PMID:17936703<ref>PMID:17936703</ref>
-
{{ABSTRACT_PUBMED_17936703}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 2o1t" style="background-color:#fffaf0;"></div>
-
[[2o1t]] is a 10 chain structure with sequence from [http://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=2O1T OCA].
+
==See Also==
==See Also==
-
*[[Endoplasmin|Endoplasmin]]
+
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
-
*[[Heat Shock Proteins|Heat Shock Proteins]]
+
== References ==
-
 
+
<references/>
-
==Reference==
+
__TOC__
-
<ref group="xtra">PMID:017936703</ref><references group="xtra"/>
+
</StructureSection>
[[Category: Canis lupus familiaris]]
[[Category: Canis lupus familiaris]]
-
[[Category: Dollins, D E.]]
+
[[Category: Large Structures]]
-
[[Category: Gewirth, D T.]]
+
[[Category: Dollins DE]]
-
[[Category: Immormino, R M.]]
+
[[Category: Gewirth DT]]
-
[[Category: Warren, J J.]]
+
[[Category: Immormino RM]]
-
[[Category: Chaperone]]
+
[[Category: Warren JJ]]
-
[[Category: Endoplasmin]]
+
-
[[Category: Gp96]]
+
-
[[Category: Grp94]]
+
-
[[Category: Hsp82]]
+
-
[[Category: Hsp90]]
+
-
[[Category: Htpg]]
+

Current revision

Structure of Middle plus C-terminal domains (M+C) of GRP94

PDB ID 2o1t

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2o1t"
Personal tools