This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1pcq

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:27, 9 December 2020

Crystal structure of groEL-groES

Structural highlights

1pcq is a 21 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Gene:	GROL OR GROEL OR MOPA OR B4143 OR C5227 OR Z5748 OR ECS5124 OR SF4297 ("Bacillus coli" Migula 1895), GROS OR GROES OR MOPB OR B4142 OR C5226 OR Z5747 OR ECS5123 OR SF4296 ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CH60_ECOLI] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600] Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600] [CH10_ECOLI] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chaudhry C, Farr GW, Todd MJ, Rye HS, Brunger AT, Adams PD, Horwich AL, Sigler PB. Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics. EMBO J. 2003 Oct 1;22(19):4877-87. PMID:14517228 doi:http://dx.doi.org/10.1093/emboj/cdg477

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pcq"

@@ Line 1: / Line 1: @@
 ==Crystal structure of groEL-groES==
-<StructureSection load='1pcq' size='340' side='right' caption='[[1pcq]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
+<StructureSection load='1pcq' size='340' side='right'caption='[[1pcq]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1pcq]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PCQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1pcq]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PCQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-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></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-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></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">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 "Bacillus coli" Migula 1895]), 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 "Bacillus coli" Migula 1895])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1pcq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pcq RCSB], [http://www.ebi.ac.uk/pdbsum/1pcq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pcq ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1pcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pcq OCA], [http://pdbe.org/1pcq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pcq RCSB], [http://www.ebi.ac.uk/pdbsum/1pcq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pcq ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 29: @@
 </div>
 <div class="pdbe-citations 1pcq" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Chaperonin|Chaperonin]]
+*[[Chaperonin 3D structures|Chaperonin 3D structures]]
 == References ==
 <references/>
@@ Line 34: / Line 38: @@
 </StructureSection>
 [[Category: Bacillus coli migula 1895]]
+[[Category: Large Structures]]
 [[Category: Adams, P D]]
 [[Category: Brunger, A T]]

1pcq

From Proteopedia

Revision as of 07:27, 9 December 2020

Crystal structure of groEL-groES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox