1pcq
From Proteopedia
(New page: 200px<br /><applet load="1pcq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pcq, resolution 2.808Å" /> '''Crystal structure o...) |
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| - | [[Image:1pcq.gif|left|200px]]<br /><applet load="1pcq" size=" | + | [[Image:1pcq.gif|left|200px]]<br /><applet load="1pcq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pcq, resolution 2.808Å" /> | caption="1pcq, resolution 2.808Å" /> | ||
'''Crystal structure of groEL-groES'''<br /> | '''Crystal structure of groEL-groES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Productive cis folding by the chaperonin GroEL is triggered by the binding | + | Productive cis folding by the chaperonin GroEL is triggered by the binding of ATP but not ADP, along with cochaperonin GroES, to the same ring as non-native polypeptide, ejecting polypeptide into an encapsulated hydrophilic chamber. We examined the specific contribution of the gamma-phosphate of ATP to this activation process using complexes of ADP and aluminium or beryllium fluoride. These ATP analogues supported productive cis folding of the substrate protein, rhodanese, even when added to already-formed, folding-inactive cis ADP ternary complexes, essentially introducing the gamma-phosphate of ATP in an independent step. Aluminium fluoride was observed to stabilize the association of GroES with GroEL, with a substantial release of free energy (-46 kcal/mol). To understand the basis of such activation and stabilization, a crystal structure of GroEL-GroES-ADP.AlF3 was determined at 2.8 A. A trigonal AlF3 metal complex was observed in the gamma-phosphate position of the nucleotide pocket of the cis ring. Surprisingly, when this structure was compared with that of the previously determined GroEL-GroES-ADP complex, no other differences were observed. We discuss the likely basis of the ability of gamma-phosphate binding to convert preformed GroEL-GroES-ADP-polypeptide complexes into the folding-active state. |
==About this Structure== | ==About this Structure== | ||
| - | 1PCQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, K, ADP and AF3 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1PCQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=AF3:'>AF3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Adams, P | + | [[Category: Adams, P D.]] |
| - | [[Category: Brunger, A | + | [[Category: Brunger, A T.]] |
[[Category: Chaudhry, C.]] | [[Category: Chaudhry, C.]] | ||
| - | [[Category: Farr, G | + | [[Category: Farr, G W.]] |
| - | [[Category: Horwich, A | + | [[Category: Horwich, A L.]] |
| - | [[Category: Rye, H | + | [[Category: Rye, H S.]] |
| - | [[Category: Sigler, P | + | [[Category: Sigler, P B.]] |
| - | [[Category: Todd, M | + | [[Category: Todd, M J.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: AF3]] | [[Category: AF3]] | ||
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[[Category: chaperone]] | [[Category: chaperone]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:31 2008'' |
Revision as of 12:27, 21 February 2008
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Crystal structure of groEL-groES
Overview
Productive cis folding by the chaperonin GroEL is triggered by the binding of ATP but not ADP, along with cochaperonin GroES, to the same ring as non-native polypeptide, ejecting polypeptide into an encapsulated hydrophilic chamber. We examined the specific contribution of the gamma-phosphate of ATP to this activation process using complexes of ADP and aluminium or beryllium fluoride. These ATP analogues supported productive cis folding of the substrate protein, rhodanese, even when added to already-formed, folding-inactive cis ADP ternary complexes, essentially introducing the gamma-phosphate of ATP in an independent step. Aluminium fluoride was observed to stabilize the association of GroES with GroEL, with a substantial release of free energy (-46 kcal/mol). To understand the basis of such activation and stabilization, a crystal structure of GroEL-GroES-ADP.AlF3 was determined at 2.8 A. A trigonal AlF3 metal complex was observed in the gamma-phosphate position of the nucleotide pocket of the cis ring. Surprisingly, when this structure was compared with that of the previously determined GroEL-GroES-ADP complex, no other differences were observed. We discuss the likely basis of the ability of gamma-phosphate binding to convert preformed GroEL-GroES-ADP-polypeptide complexes into the folding-active state.
About this Structure
1PCQ is a Protein complex structure of sequences from Escherichia coli with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics., Chaudhry C, Farr GW, Todd MJ, Rye HS, Brunger AT, Adams PD, Horwich AL, Sigler PB, EMBO J. 2003 Oct 1;22(19):4877-87. PMID:14517228
Page seeded by OCA on Thu Feb 21 14:27:31 2008
Categories: Escherichia coli | Protein complex | Adams, P D. | Brunger, A T. | Chaudhry, C. | Farr, G W. | Horwich, A L. | Rye, H S. | Sigler, P B. | Todd, M J. | ADP | AF3 | K | MG | Chaperone
