1pcq

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[[Image:1pcq.gif|left|200px]]
[[Image:1pcq.gif|left|200px]]
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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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The line below this paragraph, containing "STRUCTURE_1pcq", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AF3:ALUMINUM+FLUORIDE'>AF3</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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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|DOMAIN=
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{{STRUCTURE_1pcq| PDB=1pcq | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pcq OCA], [http://www.ebi.ac.uk/pdbsum/1pcq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pcq RCSB]</span>
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'''Crystal structure of groEL-groES'''
'''Crystal structure of groEL-groES'''
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[[Category: Sigler, P B.]]
[[Category: Sigler, P B.]]
[[Category: Todd, M J.]]
[[Category: Todd, M J.]]
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[[Category: chaperone]]
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[[Category: Chaperone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:56:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:57:58 2008''
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Revision as of 01:56, 3 May 2008

Image:1pcq.gif

Template:STRUCTURE 1pcq

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 Page seeded by OCA on Sat May 3 04:56:43 2008

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