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ClpX is a molecular chaperone which alters the shape of DNA during bacteriophage μ transposition.[1] For details see Molecular Playground/Hexameric ClpX
ADP binding site in Helicobacter pylori ClpX (PDB entry 1um8).[2]
- ↑ 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:https://dx.doi.org/10.1016/j.bbamcr.2011.06.007
- ↑ Kim DY, Kim KK. Crystal structure of ClpX molecular chaperone from Helicobacter pylori. J Biol Chem. 2003 Dec 12;278(50):50664-70. Epub 2003 Sep 26. PMID:14514695 doi:10.1074/jbc.M305882200
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3D structures of ClpX
Updated on 17-February-2019
Molecular Playground/Hexameric ClpX, 1um8, 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
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