2RSG
Solution structure of the CERT PH domain
Summary for 2RSG
| Entry DOI | 10.2210/pdb2rsg/pdb |
| NMR Information | BMRB: 11473 |
| Descriptor | Collagen type IV alpha-3-binding protein (1 entity in total) |
| Functional Keywords | pleckstrin homology, lipid transport |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q9Y5P4 |
| Total number of polymer chains | 1 |
| Total formula weight | 11180.38 |
| Authors | Sugiki, T.,Takeuchi, K.,Tokunaga, Y.,Kumagai, K.,Kawano, M.,Nishijima, M.,Hanada, K.,Takahashi, H.,Shimada, I. (deposition date: 2012-02-25, release date: 2012-08-15, Last modification date: 2024-05-15) |
| Primary citation | Sugiki, T.,Takeuchi, K.,Yamaji, T.,Takano, T.,Tokunaga, Y.,Kumagai, K.,Hanada, K.,Takahashi, H.,Shimada, I. Structural basis for the Golgi association by the pleckstrin homology domain of the ceramide trafficking protein (CERT) J.Biol.Chem., 287:33706-33718, 2012 Cited by PubMed Abstract: Ceramide transport from the endoplasmic reticulum to the Golgi apparatus is crucial in sphingolipid biosynthesis, and the process relies on the ceramide trafficking protein (CERT), which contains pleckstrin homology (PH) and StAR-related lipid transfer domains. The CERT PH domain specifically recognizes phosphatidylinositol 4-monophosphate (PtdIns(4)P), a characteristic phosphoinositide in the Golgi membrane, and is indispensable for the endoplasmic reticulum-to-Golgi transport of ceramide by CERT. In this study, we determined the three-dimensional structure of the CERT PH domain by using solution NMR techniques. The structure revealed the presence of a characteristic basic groove near the canonical PtdIns(4)P recognition site. An extensive interaction study using NMR and other biophysical techniques revealed that the basic groove coordinates the CERT PH domain for efficient PtdIns(4)P recognition and localization in the Golgi apparatus. The notion was also supported by Golgi mislocalization of the CERT mutants in living cells. The distinctive binding modes reflect the functions of PH domains, as the basic groove is conserved only in the PH domains involved with the PtdIns(4)P-dependent lipid transport activity but not in those with the signal transduction activity. PubMed: 22869376DOI: 10.1074/jbc.M112.367730 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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