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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 08-June-2021
Molecular Playground/Hexameric ClpX - MtClp N-terminal domain - Mycobacterium tuberculosis
1um8, 4i34, [[[4i5o|4i5o]], 4i63, 4i9k - EcClp - Escherichia coli
3hws, 4i4l - EcClp + ADP
4i81 - EcClp + ATPgS
6pp5 - EcClp + ADP – Cryo EM
6pp6, 6pp7, 6pp8 - EcClp + ADP + ATPgS – Cryo EM
6sfw - LmClp – Listeria monocytogenes - Cryo EM
6lsy - SpClp – Streptococcus pneumonia - Cryo EM
6lt4 - SpClp + ATPgS – Cryo EM
References
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