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ClpX
From Proteopedia
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| - | <StructureSection load='1um8' size='350' side='right' caption='Helicobacter pylori ClpX complex with ADP (PDB entry [[1um8]])' scene=''> | + | <StructureSection load='1um8' size='350' side='right' caption='Helicobacter pylori ClpX complex with ADP (PDB entry [[1um8]])' scene='45/458468/Cv/1'> |
'''Clp'''X is a molecular chaperone which alters the shape of DNA during bacteriophage μ transposition.<ref>PMID:21736903</ref> For details see [[Molecular Playground/Hexameric ClpX]] | '''Clp'''X is a molecular chaperone which alters the shape of DNA during bacteriophage μ transposition.<ref>PMID:21736903</ref> For details see [[Molecular Playground/Hexameric ClpX]] | ||
| + | <scene name='45/458468/Cv/3'>ADP binding site</scene> in ''Helicobacter pylori'' ClpX (PDB entry [[1um8]]). | ||
</StructureSection> | </StructureSection> | ||
==3D structures of ClpX== | ==3D structures of ClpX== | ||
Revision as of 14:40, 27 January 2016
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3D structures of ClpX
Updated on 27-January-2016
3hte, 4i34, 4i4l, 4i5o, 4i63, 4i9k – EcClpX residues 62-424 – Escherichia coli
3hws - EcClpX residues 62-424 (mutant) + ADP
2ds5, 2ds6, 2ds7 - EcClpX zinc-binding domain
1ovx - EcClpX zinc-binding domain - NMR
2ds8 - EcClpX zinc-binding domain + SSPB-tail peptide
4i81 – EcCLPX + ATP-γ-S
1um8 - ClpX residues 71-446 + ADP – Helicobacter pylori
References
- ↑ Baker TA, Sauer RT. ClpXP, an ATP-powered unfolding and protein-degradation machine. Biochim Biophys Acta. 2012 Jan;1823(1):15-28. doi: 10.1016/j.bbamcr.2011.06.007. , Epub 2011 Jun 27. PMID:21736903 doi:http://dx.doi.org/10.1016/j.bbamcr.2011.06.007
