5EGE
Structure of ENPP6, a choline-specific glycerophosphodiester-phosphodiesterase
Summary for 5EGE
| Entry DOI | 10.2210/pdb5ege/pdb |
| Related | 5EGH |
| Descriptor | Ectonucleotide pyrophosphatase/phosphodiesterase family member 6, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | choline metabolism, phosphodiesterase, hydrolase |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 4 |
| Total formula weight | 204818.56 |
| Authors | Morita, J.,Kano, K.,Kato, K.,Takita, H.,Ishitani, R.,Nishimasu, H.,Nureki, O.,Aoki, J. (deposition date: 2015-10-27, release date: 2016-03-09, Last modification date: 2020-07-29) |
| Primary citation | Morita, J.,Kano, K.,Kato, K.,Takita, H.,Sakagami, H.,Yamamoto, Y.,Mihara, E.,Ueda, H.,Sato, T.,Tokuyama, H.,Arai, H.,Asou, H.,Takagi, J.,Ishitani, R.,Nishimasu, H.,Nureki, O.,Aoki, J. Structure and biological function of ENPP6, a choline-specific glycerophosphodiester-phosphodiesterase Sci Rep, 6:20995-20995, 2016 Cited by PubMed Abstract: Choline is an essential nutrient for all living cells and is produced extracellularly by sequential degradation of phosphatidylcholine (PC). However, little is known about how choline is produced extracellularly. Here, we report that ENPP6, a choline-specific phosphodiesterase, hydrolyzes glycerophosphocholine (GPC), a degradation product of PC, as a physiological substrate and participates in choline metabolism. ENPP6 is highly expressed in liver sinusoidal endothelial cells and developing oligodendrocytes, which actively incorporate choline and synthesize PC. ENPP6-deficient mice exhibited fatty liver and hypomyelination, well known choline-deficient phenotypes. The choline moiety of GPC was incorporated into PC in an ENPP6-dependent manner both in vivo and in vitro. The crystal structure of ENPP6 in complex with phosphocholine revealed that the choline moiety of the phosphocholine is recognized by a choline-binding pocket formed by conserved aromatic and acidic residues. The present study provides the molecular basis for ENPP6-mediated choline metabolism at atomic, cellular and tissue levels. PubMed: 26888014DOI: 10.1038/srep20995 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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