6dju: Difference between revisions

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-'''Unreleased structure'''
-The entry 6dju is ON HOLD  until Paper Publication
+==Mtb ClpB in complex with ATPgammaS and casein, Conformer 1==
+<SX load='6dju' size='340' side='right' viewer='molstar' caption='[[6dju]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6dju]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DJU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DJU 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]] 3.8&#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>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=6dju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dju OCA], [https://pdbe.org/6dju PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dju RCSB], [https://www.ebi.ac.uk/pdbsum/6dju PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dju ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CLPB_MYCTU CLPB_MYCTU] 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 (By similarity).
-Authors:
+==See Also==
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
-Description:
+__TOC__
-[[Category: Unreleased Structures]]
+</SX>
+[[Category: Bos taurus]]
+[[Category: Large Structures]]
+[[Category: Mycobacterium tuberculosis]]
+[[Category: Li HL]]
+[[Category: Yu HJ]]