8I76
Crystal structure of decarboxylated osteocalcin at pH 2.0 without glycerol
Summary for 8I76
Entry DOI | 10.2210/pdb8i76/pdb |
Descriptor | Osteocalcin (2 entities in total) |
Functional Keywords | ca-binding protein, structural protein |
Biological source | Bos taurus (cattle) |
Total number of polymer chains | 2 |
Total formula weight | 8495.23 |
Authors | Yokoyama, T.,Nabeshima, Y.,Obita, T.,Mizuguchi, M. (deposition date: 2023-01-31, release date: 2024-01-31, Last modification date: 2024-11-13) |
Primary citation | Mizuguchi, M.,Yokoyama, T.,Otani, T.,Kuribara, S.,Nabeshima, Y.,Obita, T.,Hirata, M.,Kawano, K. Structural and mutational analyses of decarboxylated osteocalcin provide insight into its adiponectin-inducing activity. Febs Lett., 597:1479-1488, 2023 Cited by PubMed Abstract: An acidic environment in bone is essential for bone metabolism and the production of decarboxylated osteocalcin, which functions as a regulatory hormone of glucose metabolism. Here, we describe the high-resolution X-ray crystal structure of decarboxylated osteocalcin under acidic conditions. Decarboxylated osteocalcin at pH 2.0 retains the α-helix structure of native osteocalcin with three γ-carboxyglutamic acid residues at neutral pH. This implies that decarboxylated osteocalcin is stable under an acidic environment in bone. In addition, site-directed mutagenesis revealed that Glu17 and Glu21 are important for the adiponectin-inducing activity of decarboxylated osteocalcin. These findings suggest that the receptor of decarboxylated osteocalcin responds to the negative charge in helix 1 of osteocalcin. PubMed: 36976525DOI: 10.1002/1873-3468.14618 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.381 Å) |
Structure validation
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