4UR4

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

4UR4 の概要

• エントリーDOI: 10.2210/pdb4ur4/pdb
• 関連するPDBエントリー: 4UR6
• 分子名称: ANTIFREEZE PROTEIN 13 (2 entities in total)
• 機能のキーワード: antifreeze protein, fish, type iii, qae1 isoform
• 由来する生物種: ZOARCES VIVIPARUS (EUROPEAN EELPOUT, VIVIPAROUS BLENNY)
• 細胞内の位置: Secreted : A3EYI7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7122.55

構造登録者

Wilkens, C.,Poulsen, J.-C.N.,Ramloev, H.,Lo Leggio, L. (登録日: 2014-06-26, 公開日: 2014-07-23, 最終更新日: 2024-01-10)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.45 Å)