1pcq

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[[Image:1pcq.gif|left|200px]]<br /><applet load="1pcq" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1pcq.gif|left|200px]]
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caption="1pcq, resolution 2.808&Aring;" />
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'''Crystal structure of groEL-groES'''<br />
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{{Structure
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|PDB= 1pcq |SIZE=350|CAPTION= <scene name='initialview01'>1pcq</scene>, resolution 2.808&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=AF3:ALUMINUM FLUORIDE'>AF3</scene>
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|ACTIVITY=
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|GENE= GROL OR GROEL OR MOPA OR B4143 OR C5227 OR Z5748 OR ECS5124 OR SF4297 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), GROS OR GROES OR MOPB OR B4142 OR C5226 OR Z5747 OR ECS5123 OR SF4296 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Crystal structure of groEL-groES'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1PCQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCQ OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14517228 14517228]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14517228 14517228]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: chaperone]]
[[Category: chaperone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:22:43 2008''

Revision as of 11:22, 20 March 2008

Image:1pcq.gif


PDB ID 1pcq

Drag the structure with the mouse to rotate
, resolution 2.808Å
Ligands: , , and
Gene: GROL OR GROEL OR MOPA OR B4143 OR C5227 OR Z5748 OR ECS5124 OR SF4297 (Escherichia coli), GROS OR GROES OR MOPB OR B4142 OR C5226 OR Z5747 OR ECS5123 OR SF4296 (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



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. 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

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