6og2: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6og2 is ON HOLD
+==Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein, post-state==
+<SX load='6og2' size='340' side='right' viewer='molstar' caption='[[6og2]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6og2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OG2 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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=6og2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6og2 OCA], [https://pdbe.org/6og2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6og2 RCSB], [https://www.ebi.ac.uk/pdbsum/6og2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6og2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CLPB_ECOLI CLPB_ECOLI] Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK.<ref>PMID:10982797</ref> <ref>PMID:12624113</ref> <ref>PMID:14640692</ref>
-Authors: Rizo, A.R., Lin, J.-B., Gates, S.N., Tse, E., Bart, S.M., Castellano, L.M., Dimaio, F., Shorter, J., Southworth, D.R.
+==See Also==
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
-Description: Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein, post-state
+*[[3D structures of ClpB|3D structures of ClpB]]
-[[Category: Unreleased Structures]]
+== References ==
-[[Category: Southworth, D.R]]
+<references/>
-[[Category: Shorter, J]]
+__TOC__
-[[Category: Castellano, L.M]]
+</SX>
-[[Category: Dimaio, F]]
+[[Category: Escherichia coli K-12]]
-[[Category: Tse, E]]
+[[Category: Large Structures]]
-[[Category: Gates, S.N]]
+[[Category: Bart SM]]
-[[Category: Rizo, A.R]]
+[[Category: Castellano LM]]
-[[Category: Lin, J.-B]]
+[[Category: Dimaio F]]
-[[Category: Bart, S.M]]
+[[Category: Gates SN]]
+[[Category: Lin J-B]]
+[[Category: Rizo AR]]
+[[Category: Shorter J]]
+[[Category: Southworth DR]]
+[[Category: Tse E]]