4KE2
Crystal structure of the hyperactive Type I antifreeze from winter flounder
Summary for 4KE2
| Entry DOI | 10.2210/pdb4ke2/pdb |
| Descriptor | Type I hyperactive antifreeze protein (2 entities in total) |
| Functional Keywords | dimeric alpha-helical bundle, antifreeze protein |
| Biological source | Pseudopleuronectes americanus (Winter flounder) |
| Cellular location | Secreted: B1P0S1 |
| Total number of polymer chains | 3 |
| Total formula weight | 50477.01 |
| Authors | Sun, T.,Lin, F.-H.,Campbell, R.L.,Allingham, J.S.,Davies, P.L. (deposition date: 2013-04-25, release date: 2014-02-26, Last modification date: 2024-02-28) |
| Primary citation | Sun, T.,Lin, F.H.,Campbell, R.L.,Allingham, J.S.,Davies, P.L. An antifreeze protein folds with an interior network of more than 400 semi-clathrate waters. Science, 343:795-798, 2014 Cited by PubMed Abstract: When polypeptide chains fold into a protein, hydrophobic groups are compacted in the center with exclusion of water. We report the crystal structure of an alanine-rich antifreeze protein that retains ~400 waters in its core. The putative ice-binding residues of this dimeric, four-helix bundle protein point inwards and coordinate the interior waters into two intersecting polypentagonal networks. The bundle makes minimal protein contacts between helices, but is stabilized by anchoring to the semi-clathrate water monolayers through backbone carbonyl groups in the protein interior. The ordered waters extend outwards to the protein surface and likely are involved in ice binding. This protein fold supports both the anchored-clathrate water mechanism of antifreeze protein adsorption to ice and the water-expulsion mechanism of protein folding. PubMed: 24531972DOI: 10.1126/science.1247407 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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