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2MXP

Solution structure of NDP52 ubiquitin-binding zinc finger

Summary for 2MXP
Entry DOI10.2210/pdb2mxp/pdb
Related4XKL
NMR InformationBMRB: 25423
DescriptorCalcium-binding and coiled-coil domain-containing protein 2, ZINC ION (2 entities in total)
Functional Keywordszinc finger, ndp52, ubiquitin-binding, c2h2-type, metal binding protein
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm, perinuclear region : Q13137
Total number of polymer chains1
Total formula weight3952.95
Authors
Pan, L.,Xie, X. (deposition date: 2015-01-12, release date: 2015-11-11, Last modification date: 2024-05-15)
Primary citationXie, X.,Li, F.,Wang, Y.,Wang, Y.,Lin, Z.,Cheng, X.,Liu, J.,Chen, C.,Pan, L.
Molecular basis of ubiquitin recognition by the autophagy receptor CALCOCO2
Autophagy, 11:1775-1789, 2015
Cited by
PubMed 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.
PubMed: 26506893
DOI: 10.1080/15548627.2015.1082025
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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