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2N73

Solution structure of the ACBD3:PI4KB complex

Summary for 2N73
Entry DOI10.2210/pdb2n73/pdb
Related2N72
NMR InformationBMRB: 25791
DescriptorGolgi resident protein GCP60, Phosphatidylinositol 4-kinase beta (2 entities in total)
Functional Keywordskinase, transferase-transferase regulator complex, transferase/transferase regulator
Biological sourceHomo sapiens (human)
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Cellular locationGolgi apparatus membrane ; Peripheral membrane protein ; Cytoplasmic side : Q9H3P7
Total number of polymer chains2
Total formula weight16303.34
Authors
Veverka, V.,Hexnerova, R. (deposition date: 2015-09-02, release date: 2016-07-20, Last modification date: 2024-05-15)
Primary citationKlima, M.,Toth, D.J.,Hexnerova, R.,Baumlova, A.,Chalupska, D.,Tykvart, J.,Rezabkova, L.,Sengupta, N.,Man, P.,Dubankova, A.,Humpolickova, J.,Nencka, R.,Veverka, V.,Balla, T.,Boura, E.
Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein.
Sci Rep, 6:23641-23641, 2016
Cited by
PubMed Abstract: Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells. To convert their lipid substrates, PI4Ks must be recruited to the correct membrane compartment. PI4KB is critical for the maintenance of the Golgi and trans Golgi network (TGN) PI4P pools, however, the actual targeting mechanism of PI4KB to the Golgi and TGN membranes is unknown. Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3). We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.
PubMed: 27009356
DOI: 10.1038/srep23641
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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