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1tc0
From Proteopedia
(New page: 200px<br /><applet load="1tc0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tc0, resolution 2.20Å" /> '''Ligand Induced Confo...) |
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| - | [[Image:1tc0.gif|left|200px]]<br /><applet load="1tc0" size=" | + | [[Image:1tc0.gif|left|200px]]<br /><applet load="1tc0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tc0, resolution 2.20Å" /> | caption="1tc0, resolution 2.20Å" /> | ||
'''Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP'''<br /> | '''Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | GRP94 is the endoplasmic reticulum paralog of cytoplasmic Hsp90. Models of | + | GRP94 is the endoplasmic reticulum paralog of cytoplasmic Hsp90. Models of Hsp90 action posit an ATP-dependent conformational switch in the N-terminal ligand regulatory domain of the chaperone. However, crystal structures of the isolated N-domain of Hsp90 in complex with a variety of ligands have yet to demonstrate such a conformational change. We have determined the structure of the N-domain of GRP94 in complex with ATP, ADP, and AMP. Compared with the N-ethylcarboxamidoadenosine and radicicol-bound forms, these structures reveal a large conformational rearrangement in the protein. The nucleotide-bound form exposes new surfaces that interact to form a biochemically plausible dimer that is reminiscent of those seen in structures of MutL and DNA gyrase. Weak ATP binding and a conformational change in response to ligand identity are distinctive mechanistic features of GRP94 and suggest a model for how GRP94 functions in the absence of co-chaperones and ATP hydrolysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1TC0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] with MG, ATP and PG4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1TC0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=PG4:'>PG4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TC0 OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Canis lupus familiaris]] | [[Category: Canis lupus familiaris]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dollins, D | + | [[Category: Dollins, D E.]] |
| - | [[Category: Gewirth, D | + | [[Category: Gewirth, D T.]] |
| - | [[Category: Immormino, R | + | [[Category: Immormino, R M.]] |
| - | [[Category: Shaffer, P | + | [[Category: Shaffer, P L.]] |
| - | [[Category: Soldano, K | + | [[Category: Soldano, K L.]] |
| - | [[Category: Walker, M | + | [[Category: Walker, M A.]] |
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
| Line 29: | Line 29: | ||
[[Category: hsp90]] | [[Category: hsp90]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:11:58 2008'' |
Revision as of 13:11, 21 February 2008
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Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP
Overview
GRP94 is the endoplasmic reticulum paralog of cytoplasmic Hsp90. Models of Hsp90 action posit an ATP-dependent conformational switch in the N-terminal ligand regulatory domain of the chaperone. However, crystal structures of the isolated N-domain of Hsp90 in complex with a variety of ligands have yet to demonstrate such a conformational change. We have determined the structure of the N-domain of GRP94 in complex with ATP, ADP, and AMP. Compared with the N-ethylcarboxamidoadenosine and radicicol-bound forms, these structures reveal a large conformational rearrangement in the protein. The nucleotide-bound form exposes new surfaces that interact to form a biochemically plausible dimer that is reminiscent of those seen in structures of MutL and DNA gyrase. Weak ATP binding and a conformational change in response to ligand identity are distinctive mechanistic features of GRP94 and suggest a model for how GRP94 functions in the absence of co-chaperones and ATP hydrolysis.
About this Structure
1TC0 is a Single protein structure of sequence from Canis lupus familiaris with , and as ligands. Full crystallographic information is available from OCA.
Reference
Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone., Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT, J Biol Chem. 2004 Oct 29;279(44):46162-71. Epub 2004 Aug 2. PMID:15292259
Page seeded by OCA on Thu Feb 21 15:11:58 2008
Categories: Canis lupus familiaris | Single protein | Dollins, D E. | Gewirth, D T. | Immormino, R M. | Shaffer, P L. | Soldano, K L. | Walker, M A. | ATP | MG | PG4 | Atp | Bergerat | Chaperone | Endoplasmic reticulum | Grp94 | Hsp90
