1pcq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1pcq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pcq, resolution 2.808&Aring;" /> '''Crystal structure o...)
Current revision (08:07, 14 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1pcq.gif|left|200px]]<br /><applet load="1pcq" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1pcq, resolution 2.808&Aring;" />
 
-
'''Crystal structure of groEL-groES'''<br />
 
-
==Overview==
+
==Crystal structure of groEL-groES==
-
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.
+
<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 [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PCQ FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.808&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pcq OCA], [https://pdbe.org/1pcq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pcq RCSB], [https://www.ebi.ac.uk/pdbsum/1pcq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pcq ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CH60_ECOLI 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]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pc/1pcq_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pcq ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PCQ OCA].
+
*[[Chaperonin|Chaperonin]]
-
 
+
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
-
==Reference==
+
__TOC__
-
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]
+
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Protein complex]]
+
[[Category: Large Structures]]
-
[[Category: Adams, P.D.]]
+
[[Category: Adams PD]]
-
[[Category: Brunger, A.T.]]
+
[[Category: Brunger AT]]
-
[[Category: Chaudhry, C.]]
+
[[Category: Chaudhry C]]
-
[[Category: Farr, G.W.]]
+
[[Category: Farr GW]]
-
[[Category: Horwich, A.L.]]
+
[[Category: Horwich AL]]
-
[[Category: Rye, H.S.]]
+
[[Category: Rye HS]]
-
[[Category: Sigler, P.B.]]
+
[[Category: Sigler PB]]
-
[[Category: Todd, M.J.]]
+
[[Category: Todd MJ]]
-
[[Category: ADP]]
+
-
[[Category: AF3]]
+
-
[[Category: K]]
+
-
[[Category: MG]]
+
-
[[Category: chaperone]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:41:39 2007''
+

Current revision

Crystal structure of groEL-groES

PDB ID 1pcq

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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