1oel: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
New page: left|200px<br /><applet load="1oel" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oel, resolution 2.8Å" /> '''CONFORMATIONAL VARIAB...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(17 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1oel.jpg|left|200px]]<br /><applet load="1oel" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1oel, resolution 2.8&Aring;" />
'''CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION'''<br />


==Overview==
==CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION==
Improved refinement of the crystal structure of GroEL from Escherichia, coli has resulted in a complete atomic model for the first 524 residues. A, new torsion-angle dynamics method and non-crystallographic symmetry, restraints were used in the refinement. The model indicates that, conformational variability exists due to rigid-body movements between the, apical and intermediate domains of GroEL, resulting in deviations from, strict seven-fold symmetry. The regions of the protein involved in, polypeptide and GroES binding show unusually high B factors; these values, may indicate mobility or discrete disorder. The variability of these, regions may play a role in the ability of GroEL to bind a wide variety of, substrates.
<StructureSection load='1oel' size='340' side='right'caption='[[1oel]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1oel]] is a 7 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=1OEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OEL 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]] 2.8&#8491;</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=1oel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oel OCA], [https://pdbe.org/1oel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oel RCSB], [https://www.ebi.ac.uk/pdbsum/1oel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oel 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/oe/1oel_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=1oel ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1OEL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OEL OCA].
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 
__TOC__
==Reference==
</StructureSection>
Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution., Braig K, Adams PD, Brunger AT, Nat Struct Biol. 1995 Dec;2(12):1083-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8846220 8846220]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Adams, P.D.]]
[[Category: Adams PD]]
[[Category: Braig, K.]]
[[Category: Braig K]]
[[Category: Brunger, A.T.]]
[[Category: Brunger AT]]
[[Category: chaperonin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:56:03 2007''
Retrieved from "https://proteopedia.org/1oel"