4UR4

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

Summary for 4UR4

• Entry DOI: 10.2210/pdb4ur4/pdb
• Related: 4UR6
• Descriptor: ANTIFREEZE PROTEIN 13 (2 entities in total)
• Functional Keywords: antifreeze protein, fish, type iii, qae1 isoform
• Biological source: ZOARCES VIVIPARUS (EUROPEAN EELPOUT, VIVIPAROUS BLENNY)
• Cellular location: Secreted : A3EYI7
• Total number of polymer chains: 1
• Total formula weight: 7122.55

Authors

Wilkens, C.,Poulsen, J.-C.N.,Ramloev, H.,Lo Leggio, L. (deposition date: 2014-06-26, release date: 2014-07-23, Last modification date: 2024-01-10)

Primary citation

Wilkens, C.,Poulsen, J.N.,Ramlov, H.,Lo Leggio, L.
Purification, Crystal Structure Determination and Functional Characterization of Type III Antifreeze Proteins from the European Eelpout Zoarces Viviparus.
Cryobiology, 69:163-, 2014

PubMed Abstract: 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.

PubMed: 25025819
DOI: 10.1016/J.CRYOBIOL.2014.07.003

Experimental method

X-RAY DIFFRACTION (1.45 Å)