1gru: Difference between revisions

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 <SX load='1gru' size='340' side='right' viewer='molstar' caption='[[1gru]], [[Resolution|resolution]] 12.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1gru]] is a 21 chain structure with sequence from [https://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=1GRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GRU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1gru]] 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=1GRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GRU FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aon|1aon]], [[1egs|1egs]], [[1der|1der]], [[1fy9|1fy9]], [[1fya|1fya]], [[1gr5|1gr5]], [[1gr6|1gr6]], [[1grl|1grl]], [[1jon|1jon]], [[1kid|1kid]], [[1oel|1oel]]</div></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]] 12.5&#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=1gru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gru OCA], [https://pdbe.org/1gru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gru RCSB], [https://www.ebi.ac.uk/pdbsum/1gru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gru 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] [[https://www.uniprot.org/uniprot/CH10_ECOLI CH10_ECOLI]] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580]
+[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]]
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 </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=1gru ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of its two rings, priming that ring to become folding-active upon GroES binding, while simultaneously discharging the previous folding chamber from the opposite ring. The GroEL-ATP structure, determined by cryo-EM and atomic structure fitting, shows that the intermediate domains rotate downward, switching their intersubunit salt bridge contacts from substrate binding to ATP binding domains. These observations, together with the effects of ATP binding to a GroEL-GroES-ADP complex, suggest structural models for the ATP-induced reduction in affinity for polypeptide and for cooperativity. The model for cooperativity, based on switching of intersubunit salt bridge interactions around the GroEL ring, may provide general insight into cooperativity in other ring complexes and molecular machines.
-ATP-bound states of GroEL captured by cryo-electron microscopy.,Ranson NA, Farr GW, Roseman AM, Gowen B, Fenton WA, Horwich AL, Saibil HR Cell. 2001 Dec 28;107(7):869-79. PMID:11779463<ref>PMID:11779463</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1gru" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Chaperonin 3D structures|Chaperonin 3D structures]]
 *[[Heat Shock Protein structures|Heat Shock Protein structures]]
-== References ==
-<references/>
 __TOC__
 </SX>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Farr, G W]]
+[[Category: Farr GW]]
-[[Category: Fenton, W A]]
+[[Category: Fenton WA]]
-[[Category: Gowen, B]]
+[[Category: Gowen B]]
-[[Category: Horwich, A L]]
+[[Category: Horwich AL]]
-[[Category: Ranson, N A]]
+[[Category: Ranson NA]]
-[[Category: Roseman, A M]]
+[[Category: Roseman AM]]
-[[Category: Saibil, H R]]
+[[Category: Saibil HR]]
-[[Category: Adp]]
-[[Category: Chaperone]]
-[[Category: Chaperonin]]
-[[Category: Hsp60]]
-[[Category: Molecular chaperone]]
-[[Category: Roe]]