1oel

<StructureSection load='1oel' size='340' side='right' caption='[[1oel]], [[Resolution|resolution]] 2.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[1oel]] is a 7 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=1OEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OEL FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GROEL ([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=1oel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oel OCA], [http://pdbe.org/1oel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oel RCSB], [http://www.ebi.ac.uk/pdbsum/1oel PDBsum]</span></td></tr>

[[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]

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oe/1oel_consurf.spt"</scriptWhenChecked>

</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].

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== Publication Abstract from PubMed ==

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.

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:8846220<ref>PMID:8846220</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1oel" style="background-color:#fffaf0;"></div>

*[[Heat Shock Proteins|Heat Shock Proteins]]

[[Category: Bacillus coli migula 1895]]

[[Category: Adams, P D]]

[[Category: Braig, K]]

[[Category: Brunger, A T]]

[[Category: Chaperonin]]