5UYT
Crystal structure of ice binding protein from an Antarctic bacterium Flavobacteriaceae
Summary for 5UYT
| Entry DOI | 10.2210/pdb5uyt/pdb |
| Descriptor | Ice-binding protein, NITRATE ION (3 entities in total) |
| Functional Keywords | antifreeze protein, ice binding protein, right-handed beta-helix, beta-solenoid |
| Biological source | Flavobacteriaceae bacterium |
| Total number of polymer chains | 2 |
| Total formula weight | 105632.26 |
| Authors | Wang, C.,Pakhomova, S.,Newcomer, M.E.,Christner, B.C.,Luo, B.-H. (deposition date: 2017-02-24, release date: 2017-10-25, Last modification date: 2024-11-13) |
| Primary citation | Wang, C.,Pakhomova, S.,Newcomer, M.E.,Christner, B.C.,Luo, B.H. Structural basis of antifreeze activity of a bacterial multi-domain antifreeze protein. PLoS ONE, 12:e0187169-e0187169, 2017 Cited by PubMed Abstract: Antifreeze proteins (AFPs) enhance the survival of organisms inhabiting cold environments by affecting the formation and/or structure of ice. We report the crystal structure of the first multi-domain AFP that has been characterized. The two ice binding domains are structurally similar. Each consists of an irregular β-helix with a triangular cross-section and a long α-helix that runs parallel on one side of the β-helix. Both domains are stabilized by hydrophobic interactions. A flat plane on the same face of each domain's β-helix was identified as the ice binding site. Mutating any of the smaller residues on the ice binding site to bulkier ones decreased the antifreeze activity. The bulky side chain of Leu174 in domain A sterically hinders the binding of water molecules to the protein backbone, partially explaining why antifreeze activity by domain A is inferior to that of domain B. Our data provide a molecular basis for understanding differences in antifreeze activity between the two domains of this protein and general insight on how structural differences in the ice-binding sites affect the activity of AFPs. PubMed: 29108002DOI: 10.1371/journal.pone.0187169 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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