6ed3
From Proteopedia
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==Mtb ClpB in complex with AMPPNP== | ==Mtb ClpB in complex with AMPPNP== | ||
| - | < | + | <SX load='6ed3' size='340' side='right' viewer='molstar' caption='[[6ed3]], [[Resolution|resolution]] 6.30Å' scene=''> |
== Structural highlights == | == 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 [ | + | <table><tr><td colspan='2'>[[6ed3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6ED3 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.3Å</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=6ed3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ed3 OCA], [https://pdbe.org/6ed3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ed3 RCSB], [https://www.ebi.ac.uk/pdbsum/6ed3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ed3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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). |
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| + | ==See Also== | ||
| + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
| + | *[[3D structures of ClpB|3D structures of ClpB]] | ||
__TOC__ | __TOC__ | ||
| - | </ | + | </SX> |
| - | [[Category: | + | [[Category: Large Structures]] |
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[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
| - | [[Category: | + | [[Category: Li HL]] |
| - | [[Category: | + | [[Category: Yu HJ]] |
Current revision
Mtb ClpB in complex with AMPPNP
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