This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


6og1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:24, 20 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
==Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein, pre-state==
==Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein, pre-state==
-
<StructureSection load='6og1' size='340' side='right'caption='[[6og1]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+
<SX load='6og1' size='340' side='right' viewer='molstar' caption='[[6og1]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6og1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OG1 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6og1]] 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=6OG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OG1 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene></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]] 3.3&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6og2|6og2]], [[6og3|6og3]], [[6oax|6oax]], [[6oay|6oay]]</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>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene></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=6og1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6og1 OCA], [http://pdbe.org/6og1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6og1 RCSB], [http://www.ebi.ac.uk/pdbsum/6og1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6og1 ProSAT]</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=6og1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6og1 OCA], [https://pdbe.org/6og1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6og1 RCSB], [https://www.ebi.ac.uk/pdbsum/6og1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6og1 ProSAT]</span></td></tr>
</table>
</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>
 +
 +
==See Also==
 +
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 +
*[[3D structures of ClpB|3D structures of ClpB]]
 +
== References ==
 +
<references/>
__TOC__
__TOC__
-
</StructureSection>
+
</SX>
 +
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Bart, S M]]
+
[[Category: Bart SM]]
-
[[Category: Castellano, L M]]
+
[[Category: Castellano LM]]
-
[[Category: Dimaio, F]]
+
[[Category: Dimaio F]]
-
[[Category: Gates, S N]]
+
[[Category: Gates SN]]
-
[[Category: Lin, J B]]
+
[[Category: Lin J-B]]
-
[[Category: Rizo, A R]]
+
[[Category: Rizo AR]]
-
[[Category: Shorter, J]]
+
[[Category: Shorter J]]
-
[[Category: Southworth, D R]]
+
[[Category: Southworth DR]]
-
[[Category: Tse, E]]
+
[[Category: Tse E]]
-
[[Category: Aaa+]]
+
-
[[Category: Chaperone]]
+
-
[[Category: Clpb]]
+
-
[[Category: Disaggregase]]
+

Current revision

Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein, pre-state

6og1, resolution 3.30Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools