3cau: Difference between revisions

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==D7 symmetrized structure of unliganded GroEL at 4.2 Angstrom resolution by cryoEM==
==D7 symmetrized structure of unliganded GroEL at 4.2 Angstrom resolution by cryoEM==
<StructureSection load='3cau' size='340' side='right' caption='[[3cau]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
<SX load='3cau' size='340' side='right' viewer='molstar' caption='[[3cau]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3cau]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CAU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CAU FirstGlance]. <br>
<table><tr><td colspan='2'>[[3cau]] 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=3CAU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CAU FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3c9v|3c9v]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.2&#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=3cau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cau OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cau RCSB], [http://www.ebi.ac.uk/pdbsum/3cau PDBsum]</span></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=3cau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cau OCA], [https://pdbe.org/3cau PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cau RCSB], [https://www.ebi.ac.uk/pdbsum/3cau PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cau ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ca/3cau_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ca/3cau_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=3cau ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In this work, we employ single-particle electron cryo-microscopy (cryo-EM) to reconstruct GroEL to approximately 4 A resolution with both D7 and C7 symmetry. Using a newly developed skeletonization algorithm and secondary structure element identification in combination with sequence-based secondary structure prediction, we demonstrate that it is possible to achieve a de novo Calpha trace directly from a cryo-EM reconstruction. The topology of our backbone trace is completely accurate, though subtle alterations illustrate significant differences from existing crystal structures. In the map with C7 symmetry, the seven monomers in each ring are identical; however, the subunits have a subtly different structure in each ring, particularly in the equatorial domain. These differences include an asymmetric salt bridge, density in the nucleotide-binding pocket of only one ring, and small shifts in alpha helix positions. This asymmetric conformation is different from previous asymmetric structures, including GroES-bound GroEL, and may represent a "primed state" in the chaperonin pathway.
De novo backbone trace of GroEL from single particle electron cryomicroscopy.,Ludtke SJ, Baker ML, Chen DH, Song JL, Chuang DT, Chiu W Structure. 2008 Mar;16(3):441-8. PMID:18334219<ref>PMID:18334219</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Chaperonin|Chaperonin]]
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Baker, M L]]
[[Category: Escherichia coli]]
[[Category: Chen, D H]]
[[Category: Large Structures]]
[[Category: Chiu, W]]
[[Category: Baker ML]]
[[Category: Chuang, D]]
[[Category: Chen DH]]
[[Category: Ludtke, S J]]
[[Category: Chiu W]]
[[Category: Song, J L]]
[[Category: Chuang D]]
[[Category: Atp-binding]]
[[Category: Ludtke SJ]]
[[Category: Cell cycle]]
[[Category: Song JL]]
[[Category: Cell division]]
[[Category: Chaperone]]
[[Category: Groel]]
[[Category: Nucleotide-binding]]
[[Category: Phosphoprotein]]

Latest revision as of 12:34, 21 February 2024

D7 symmetrized structure of unliganded GroEL at 4.2 Angstrom resolution by cryoEMD7 symmetrized structure of unliganded GroEL at 4.2 Angstrom resolution by cryoEM

3cau, resolution 4.20Å

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