1xck

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of apo GroEL

Structural highlights

1xck is a 14 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.92Å
Ligands:	, , ,
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]

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

The 2.9A resolution crystal structure of apo wild-type GroEL was determined for the first time and represents the reference structure, facilitating the study of structural and functional differences observed in GroEL variants. Until now the crystal structure of the mutant Arg13Gly, Ala126Val GroEL was used for this purpose. We show that, due to the mutations as well as to the presence of a crystallographic symmetry, the ring-ring interface was inaccurately described. Analysis of the present structure allowed the definition of structural elements at this interface, essential for understanding the inter-ring allosteric signal transmission. We also show unambiguously that there is no ATP-induced 102 degrees rotation of the apical domain helix I around its helical axis, as previously assumed in the crystal structure of the (GroEL-KMgATP)(14) complex, and analyze the apical domain movements. These results enabled us to compare our structure with other GroEL crystal structures already published, allowing us to suggest a new route through which the allosteric signal for negative cooperativity propagates within the molecule. The proposed mechanism, supported by known mutagenesis data, underlines the importance of the switching of salt bridges.

Crystal structure of wild-type chaperonin GroEL.,Bartolucci C, Lamba D, Grazulis S, Manakova E, Heumann H J Mol Biol. 2005 Dec 9;354(4):940-51. Epub 2005 Oct 21. PMID:16288915^[1]

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

References

↑ Bartolucci C, Lamba D, Grazulis S, Manakova E, Heumann H. Crystal structure of wild-type chaperonin GroEL. J Mol Biol. 2005 Dec 9;354(4):940-51. Epub 2005 Oct 21. PMID:16288915 doi:10.1016/j.jmb.2005.09.096

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/1xck"

@@ Line 1: / Line 1: @@
 ==Crystal structure of apo GroEL==
-<StructureSection load='1xck' size='340' side='right' caption='[[1xck]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
+<StructureSection load='1xck' size='340' side='right'caption='[[1xck]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1xck]] is a 14 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=1XCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XCK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1xck]] is a 14 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=1XCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XCK FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.92&#8491;</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=1xck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xck OCA], [http://pdbe.org/1xck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xck RCSB], [http://www.ebi.ac.uk/pdbsum/1xck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xck ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1xck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xck OCA], [https://pdbe.org/1xck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xck RCSB], [https://www.ebi.ac.uk/pdbsum/1xck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xck ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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]
+[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]]
@@ Line 30: / Line 31: @@
 ==See Also==
-*[[Chaperonin|Chaperonin]]
+*[[Chaperonin 3D structures|Chaperonin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Bartolucci, C]]
+[[Category: Large Structures]]
-[[Category: Grazulis, S]]
+[[Category: Bartolucci C]]
-[[Category: Heumann, H]]
+[[Category: Grazulis S]]
-[[Category: Lamba, D]]
+[[Category: Heumann H]]
-[[Category: Manakova, E]]
+[[Category: Lamba D]]
-[[Category: Chaperone]]
+[[Category: Manakova E]]
-[[Category: Chaperonin]]

1xck

From Proteopedia

Current revision

Crystal structure of apo GroEL

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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