1vzm
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Osteocalcin is a small (45 amino acids) secreted protein found to, accumulate in bone and dentin of many organisms by interacting with, calcium and hydroxyapatite, through the presence of three, gamma-carboxylated residues. In this work, we describe the first X-ray, crystal structure for a nonmammalian osteocalcin, obtained at 1.4 A, resolution, purified from the marine teleost fish Argyrosomus regius. The, three-dimensional fit between the A. regius structure and that of the only, other known X-ray structure, the porcine osteocalcin, revealed a, superposition of the Calpha atoms of their metal chelating residues, Gla, and Asp, showing that their spatial distribution is consistent with the, interatomic distances of calcium cations in the hydroxyapatite crystals., In both structures, the ... | + | Osteocalcin is a small (45 amino acids) secreted protein found to, accumulate in bone and dentin of many organisms by interacting with, calcium and hydroxyapatite, through the presence of three, gamma-carboxylated residues. In this work, we describe the first X-ray, crystal structure for a nonmammalian osteocalcin, obtained at 1.4 A, resolution, purified from the marine teleost fish Argyrosomus regius. The, three-dimensional fit between the A. regius structure and that of the only, other known X-ray structure, the porcine osteocalcin, revealed a, superposition of the Calpha atoms of their metal chelating residues, Gla, and Asp, showing that their spatial distribution is consistent with the, interatomic distances of calcium cations in the hydroxyapatite crystals., In both structures, the protein forms a tight globular arrangement of, their three alpha-helices while the remaining residues, at N- and, C-terminal regions, have essentially no secondary structure, characteristics. This study revealed the presence of a fourth, gamma-carboxylation at Glu(25), not previously detected in the structure, of the porcine osteocalcin or in any other of the sequentially, characterized mammalian osteocalcins (human, cow, and rat). A confirmation, of the fourth Gla residue in A. regius osteocalcin was achieved via LC-MS, analysis. These four doubly charged residues are, together with Asp(24), concentrated in a common surface region located on the same side of the, molecule. This further suggests that the known high affinity of, osteocalcin for bone mineral may be derived from the clustering of calcium, binding sites on this surface of the molecules. |
==About this Structure== | ==About this Structure== | ||
| - | 1VZM is a | + | 1VZM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Argyrosomus_regius Argyrosomus regius] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VZM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: vitamin k]] | [[Category: vitamin k]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:20:01 2007'' |
Revision as of 13:14, 5 November 2007
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OSTEOCALCIN FROM FISH ARGYROSOMUS REGIUS
Overview
Osteocalcin is a small (45 amino acids) secreted protein found to, accumulate in bone and dentin of many organisms by interacting with, calcium and hydroxyapatite, through the presence of three, gamma-carboxylated residues. In this work, we describe the first X-ray, crystal structure for a nonmammalian osteocalcin, obtained at 1.4 A, resolution, purified from the marine teleost fish Argyrosomus regius. The, three-dimensional fit between the A. regius structure and that of the only, other known X-ray structure, the porcine osteocalcin, revealed a, superposition of the Calpha atoms of their metal chelating residues, Gla, and Asp, showing that their spatial distribution is consistent with the, interatomic distances of calcium cations in the hydroxyapatite crystals., In both structures, the protein forms a tight globular arrangement of, their three alpha-helices while the remaining residues, at N- and, C-terminal regions, have essentially no secondary structure, characteristics. This study revealed the presence of a fourth, gamma-carboxylation at Glu(25), not previously detected in the structure, of the porcine osteocalcin or in any other of the sequentially, characterized mammalian osteocalcins (human, cow, and rat). A confirmation, of the fourth Gla residue in A. regius osteocalcin was achieved via LC-MS, analysis. These four doubly charged residues are, together with Asp(24), concentrated in a common surface region located on the same side of the, molecule. This further suggests that the known high affinity of, osteocalcin for bone mineral may be derived from the clustering of calcium, binding sites on this surface of the molecules.
About this Structure
1VZM is a Single protein structure of sequence from Argyrosomus regius with MG as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Structural evidence of a fourth Gla residue in fish osteocalcin: biological implications., Frazao C, Simes DC, Coelho R, Alves D, Williamson MK, Price PA, Cancela ML, Carrondo MA, Biochemistry. 2005 Feb 1;44(4):1234-42. PMID:15667217
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