1WFA
WINTER FLOUNDER ANTIFREEZE PROTEIN ISOFORM HPLC6 AT 4 DEGREES C
Summary for 1WFA
| Entry DOI | 10.2210/pdb1wfa/pdb |
| Related | 1WFB |
| Descriptor | ANTIFREEZE PROTEIN ISOFORM HPLC6 (2 entities in total) |
| Functional Keywords | ice binding protein, thermal hysteresis protein, antifreeze polypeptide |
| Biological source | Pseudopleuronectes americanus (winter flounder) |
| Cellular location | Secreted, extracellular space: P04002 |
| Total number of polymer chains | 2 |
| Total formula weight | 6484.98 |
| Authors | Yang, D.S.C.,Sicheri, F. (deposition date: 1995-04-03, release date: 1995-06-03, Last modification date: 2024-11-13) |
| Primary citation | Sicheri, F.,Yang, D.S. Ice-binding structure and mechanism of an antifreeze protein from winter flounder. Nature, 375:427-431, 1995 Cited by PubMed Abstract: Antifreeze proteins provide fish with protection against the freezing effect of polar environments by binding to ice surfaces and inhibiting growth of ice crystals. We present the X-ray crystal structure at 1.5 A resolution of a lone alpha-helical antifreeze protein from winter flounder, which provides a detailed look at its ice-binding features. These consist of four repeated ice-binding motifs, the side chains of which are inherently rigid or restrained by pair-wise side-chain interactions to form a flat binding surface. Elaborate amino- and carboxy-terminal cap structures are also present, which explain the protein's rich alpha-helical content in solution. We propose an ice-binding model that accounts for the binding specificity of the antifreeze protein along the <0112> axes of the (2021) ice planes. PubMed: 7760940DOI: 10.1038/375427a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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