6ed3: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6ed3 is ~~ON HOLD until Paper Publication~~

==Mtb ClpB in complex with AMPPNP==

~~Authors~~:

== Structural highlights ==

<table><tr><td colspan='2'>[[6ed3]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ED3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ED3 FirstGlance]. <br>

~~Description~~:

</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=6ed3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ed3 OCA], [http://pdbe.org/6ed3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ed3 RCSB], [http://www.ebi.ac.uk/pdbsum/6ed3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ed3 ProSAT]</span></td></tr>

[[Category: ~~Unreleased Structures~~]]

</table>

== Function ==

[[http://www.uniprot.org/uniprot/CLPB_MYCTO CLPB_MYCTO]] 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).

__TOC__

</StructureSection>

[[Category: Li, H L]]

[[Category: Yu, H J]]

[[Category: Aaa atpase]]

[[Category: Chaperone]]

[[Category: Cryoem]]

[[Category: Mycobacterium tuberculosis]]

[[Category: Pathogen]]

[[Category: Unfoldase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6ed3 is ON HOLD  until Paper Publication
+==Mtb ClpB in complex with AMPPNP==
+<StructureSection load='6ed3' size='340' side='right' caption='[[6ed3]], [[Resolution|resolution]] 6.30&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6ed3]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ED3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ED3 FirstGlance]. <br>
-Description:
+</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=6ed3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ed3 OCA], [http://pdbe.org/6ed3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ed3 RCSB], [http://www.ebi.ac.uk/pdbsum/6ed3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ed3 ProSAT]</span></td></tr>
-[[Category: Unreleased Structures]]
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CLPB_MYCTO CLPB_MYCTO]] 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).
+__TOC__
+</StructureSection>
+[[Category: Li, H L]]
+[[Category: Yu, H J]]
+[[Category: Aaa atpase]]
+[[Category: Chaperone]]
+[[Category: Cryoem]]
+[[Category: Mycobacterium tuberculosis]]
+[[Category: Pathogen]]
+[[Category: Unfoldase]]