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PDBsum entry 4xkl

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Top Page protein ligands metals Protein-protein interface(s) links
Protein binding/metal binding protein PDB id
4xkl
Contents
Protein chains
78 a.a.
30 a.a.
31 a.a.
Ligands
GOL ×2
ACT ×4
Metals
_ZN ×2
Waters ×106

References listed in PDB file
Key reference
Title Molecular basis of ubiquitin recognition by the autophagy receptor calcoco2.
Authors X.Xie, F.Li, Y.Wang, Y.Wang, Z.Lin, X.Cheng, J.Liu, C.Chen, L.Pan.
Ref. Autophagy, 2015, 11, 1775-1789. [DOI no: 10.1080/15548627.2015.1082025]
PubMed id 26506893
Abstract
The autophagy receptor CALCOCO2/NDP52 functions as a bridging adaptor and plays an essential role in the selective autophagic degradation of invading pathogens by specifically recognizing ubiquitin-coated intracellular pathogens and subsequently targeting them to the autophagic machinery; thereby it is required for innate immune defense against a range of infectious pathogens in mammals. However, the mechanistic basis underlying CALCOCO2-mediated specific recognition of ubiqutinated pathogens is still unknown. Here, using biochemical and structural analyses, we demonstrated that the cargo-binding region of CALCOCO2 contains a dynamic unconventional zinc finger as well as a C2H2-type zinc-finger, and only the C2H2-type zinc finger specifically recognizes mono-ubiquitin or poly-ubiquitin chains. In addition to elucidating the specific ubiquitin recognition mechanism of CALCOCO2, the structure of the CALCOCO2 C2H2-type zinc finger in complex with mono-ubiquitin also uncovers a unique zinc finger-binding mode for ubiquitin. Our findings provide mechanistic insight into how CALCOCO2 targets ubiquitin-decorated pathogens for autophagic degradations.
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