4ur4

Structure of the type III fish antifreeze protein from Zoarces viviparus ZvAFP13

spinqualitylabelsall models 4ur4, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ur4 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4ur6 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Antifreeze proteins (AFPs) are essential components of many organisms adaptation to cold temperatures. Fish type III AFPs are divided into two groups, SP isoforms being much less active than QAE1 isoforms. Two type III AFPs from Zoarces viviparus, a QAE1 (ZvAFP13) and an SP (ZvAFP6) isoform, are here characterized and their crystal structures determined. We conclude that the higher activity of the QAE1 isoforms cannot be attributed to single residues, but rather a combination of structural effects. Furthermore both ZvAFP6 and ZvAFP13 crystal structures have water molecules around T18 equivalent to the tetrahedral-like waters previously identified in a neutron crystal structure. Interestingly, ZvAFP6 forms dimers in the crystal, with a significant dimer interface. The presence of ZvAFP6 dimers was confirmed in solution by native electrophoresis and gel filtration. To our knowledge this is the first report of dimerization of AFP type III proteins. Purification, crystal structure determination and functional characterization of type III antifreeze proteins from the European eelpout Zoarces viviparus.,Wilkens C, Poulsen JC, Ramlov H, Leggio LL Cryobiology. 2014 Jul 12. pii: S0011-2240(14)00133-3. doi:, 10.1016/j.cryobiol.2014.07.003. PMID:25025819 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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