scholarly journals Hyperactive antifreeze protein from an Antarctic sea ice bacteriumColwelliasp. has a compound ice-binding site without repetitive sequences

FEBS Journal ◽  
2014 ◽  
Vol 281 (16) ◽  
pp. 3576-3590 ◽  
Author(s):  
Yuichi Hanada ◽  
Yoshiyuki Nishimiya ◽  
Ai Miura ◽  
Sakae Tsuda ◽  
Hidemasa Kondo
Keyword(s):  
Sea Ice ◽  
Binding Site ◽  
Repetitive Sequences ◽  
Antifreeze Protein ◽  
Antarctic Sea Ice ◽  
Ice Binding

Investigation of the Ice-Binding Site of an Insect Antifreeze Protein Using Sum-Frequency Generation Spectroscopy

2015 ◽  
Vol 6 (7) ◽  
pp. 1162-1167 ◽  
Author(s):  
Konrad Meister ◽  
Stephan Lotze ◽  
Luuk L. C. Olijve ◽  
Arthur L. DeVries ◽  
John G. Duman ◽  
...  
Keyword(s):  
Binding Site ◽  
Antifreeze Protein ◽  
Sum Frequency Generation ◽  
Sum Frequency ◽  
Sum Frequency Generation Spectroscopy ◽  
Ice Binding ◽  
Frequency Generation

scholarly journals In situ expression of eukaryotic ice-binding proteins in microbial communities of Arctic and Antarctic sea ice

2015 ◽  
Vol 9 (11) ◽  
pp. 2537-2540 ◽  
Author(s):  
Christiane Uhlig ◽  
Fabian Kilpert ◽  
Stephan Frickenhaus ◽  
Jessica U Kegel ◽  
Andreas Krell ◽  
...  
Keyword(s):  
Sea Ice ◽  
Microbial Communities ◽  
Binding Proteins ◽  
Antarctic Sea Ice ◽  
Ice Binding

Antifreeze Protein from Freeze-Tolerant Grass Has a Beta-Roll Fold with an Irregularly Structured Ice-Binding Site

2012 ◽  
Vol 416 (5) ◽  
pp. 713-724 ◽  
Author(s):  
Adam J. Middleton ◽  
Christopher B. Marshall ◽  
Frédérick Faucher ◽  
Maya Bar-Dolev ◽  
Ido Braslavsky ◽  
...  
Keyword(s):  
Binding Site ◽  
Antifreeze Protein ◽  
Ice Binding ◽  
Freeze Tolerant

The Ice-Binding Site of Sea Raven Antifreeze Protein Is Distinct from the Carbohydrate-Binding Site of the Homologous C-Type Lectin†

Biochemistry ◽  
1998 ◽  
Vol 37 (51) ◽  
pp. 17745-17753 ◽  
Author(s):  
Michèle C. Loewen ◽  
Wolfram Gronwald ◽  
Frank D. Sönnichsen ◽  
Brian D. Sykes ◽  
Peter L. Davies
Keyword(s):  
Binding Site ◽  
Antifreeze Protein ◽  
Carbohydrate Binding ◽  
Ice Binding ◽  
Sea Raven ◽  
Carbohydrate Binding Site

scholarly journals Ice-binding site of surface-bound type III antifreeze protein partially decoupled from water

2018 ◽  
Vol 20 (42) ◽  
pp. 26926-26933 ◽  
Author(s):  
Dominique Verreault ◽  
Sarah Alamdari ◽  
Steven J. Roeters ◽  
Ravindra Pandey ◽  
Jim Pfaendtner ◽  
...  
Keyword(s):  
Binding Site ◽  
Antifreeze Proteins ◽  
Antifreeze Protein ◽  
Water Interface ◽  
Native State ◽  
Type Iii ◽  
Ice Binding ◽  
Air Water Interface

Combined SFG/MD analysis together with spectral calculations revealed that type III antifreeze proteins adsorbed at the air–water interface maintains a native state and adopts an orientation that leads to a partial decoupling of its ice-binding site from water.

The Ice-Binding Site of Atlantic Herring Antifreeze Protein Corresponds to the Carbohydrate-Binding Site of C-Type Lectins†

Biochemistry ◽  
1998 ◽  
Vol 37 (12) ◽  
pp. 4080-4085 ◽  
Author(s):  
K. Vanya Ewart ◽  
Zhengjun Li ◽  
Daniel S. C. Yang ◽  
Garth L. Fletcher ◽  
Choy L. Hew
Keyword(s):  
Binding Site ◽  
Antifreeze Protein ◽  
Carbohydrate Binding ◽  
Atlantic Herring ◽  
Ice Binding ◽  
Carbohydrate Binding Site

scholarly journals Ice-binding site of snow mold fungus antifreeze protein deviates from structural regularity and high conservation

2012 ◽  
Vol 109 (24) ◽  
pp. 9360-9365 ◽  
Author(s):  
H. Kondo ◽  
Y. Hanada ◽  
H. Sugimoto ◽  
T. Hoshino ◽  
C. P. Garnham ◽  
...  
Keyword(s):  
Binding Site ◽  
Antifreeze Protein ◽  
Snow Mold ◽  
Ice Binding ◽  
Structural Regularity ◽  
Mold Fungus ◽  
High Conservation

scholarly journals Preordering of water is not needed for ice recognition by hyperactive antifreeze proteins

2018 ◽  
Vol 115 (33) ◽  
pp. 8266-8271 ◽  
Author(s):  
Arpa Hudait ◽  
Daniel R. Moberg ◽  
Yuqing Qiu ◽  
Nathan Odendahl ◽  
Francesco Paesani ◽  
...  
Keyword(s):  
Binding Site ◽  
Raman Spectra ◽  
Antifreeze Proteins ◽  
Antifreeze Protein ◽  
Bulk Liquid ◽  
Cold Environments ◽  
Ice Surface ◽  
Ice Binding ◽  
Binding Surface ◽  
Optimal Candidate

Antifreeze proteins (AFPs) inhibit ice growth in organisms living in cold environments. Hyperactive insect AFPs are particularly effective, binding ice through “anchored clathrate” motifs. It has been hypothesized that the binding of hyperactive AFPs to ice is facilitated by preordering of water at the ice-binding site (IBS) of the protein in solution. The antifreeze proteinTmAFP displays the best matching of its binding site to ice, making it the optimal candidate to develop ice-like order in solution. Here we use multiresolution simulations to unravel the mechanism by whichTmAFP recognizes and binds ice. We find that water at the IBS of the antifreeze protein in solution does not acquire ice-like or anchored clathrate-like order. Ice recognition occurs by slow diffusion of the protein to achieve the proper orientation with respect to the ice surface, followed by fast collective organization of the hydration water at the IBS to form an anchored clathrate motif that latches the protein to the ice surface. The simulations suggest that anchored clathrate order could develop on the large ice-binding surfaces of aggregates of ice-nucleating proteins (INP). We compute the infrared and Raman spectra of water in the anchored clathrate motif. The signatures of the OH stretch of water in the anchored clathrate motif can be distinguished from those of bulk liquid in the Raman spectra, but not in the infrared spectra. We thus suggest that Raman spectroscopy may be used to probe the anchored clathrate order at the ice-binding surface of INP aggregates.

scholarly journals An ice-binding protein from an Antarctic sea ice bacterium

2007 ◽  
Vol 61 (2) ◽  
pp. 214-221 ◽  
Author(s):  
James A. Raymond ◽  
Christian Fritsen ◽  
Kate Shen
Keyword(s):  
Sea Ice ◽  
Binding Protein ◽  
Antarctic Sea Ice ◽  
Ice Binding ◽  
Ice Binding Protein

scholarly journals Calcium-Binding Generates the Semi-Clathrate Waters on a Type II Antifreeze Protein to Adsorb onto an Ice Crystal Surface

Biomolecules ◽  
2019 ◽  
Vol 9 (5) ◽  
pp. 162 ◽  
Author(s):  
Tatsuya Arai ◽  
Yoshiyuki Nishimiya ◽  
Yasushi Ohyama ◽  
Hidemasa Kondo ◽  
Sakae Tsuda
Keyword(s):  
Binding Site ◽  
Calcium Binding ◽  
Crystal Surface ◽  
Hydration Shell ◽  
Antifreeze Protein ◽  
Bound State ◽  
Ice Crystal ◽  
Prism Plane ◽  
Ice Binding ◽  
Significant Difference

Hydration is crucial for a function and a ligand recognition of a protein. The hydration shell constructed on an antifreeze protein (AFP) contains many organized waters, through which AFP is thought to bind to specific ice crystal planes. For a Ca2+-dependent species of AFP, however, it has not been clarified how 1 mol of Ca2+-binding is related with the hydration and the ice-binding ability. Here we determined the X-ray crystal structure of a Ca2+-dependent AFP (jsAFP) from Japanese smelt, Hypomesus nipponensis, in both Ca2+-bound and -free states. Their overall structures were closely similar (Root mean square deviation (RMSD) of Cα = 0.31 Å), while they exhibited a significant difference around their Ca2+-binding site. Firstly, the side-chains of four of the five Ca2+-binding residues (Q92, D94 E99, D113, and D114) were oriented to be suitable for ice binding only in the Ca2+-bound state. Second, a Ca2+-binding loop consisting of a segment D94–E99 becomes less flexible by the Ca2+-binding. Third, the Ca2+-binding induces a generation of ice-like clathrate waters around the Ca2+-binding site, which show a perfect position-match to the waters constructing the first prism plane of a single ice crystal. These results suggest that generation of ice-like clathrate waters induced by Ca2+-binding enables the ice-binding of this protein.

Sign in / Sign up

Export Citation Format

Share Document