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Structural Basis for Antifreeze Activity of Ice-binding Protein from Arctic Yeast

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Title
Structural Basis for Antifreeze Activity of Ice-binding Protein from Arctic Yeast
Other Titles
북극 효모 유래 결빙방지단백질 (LeIBP) 의 구조-기능 상관관계 연구
Authors
Kim, Hak Jun
Sang Hyun Moh
Lee, Jun Hyuck
Young Min Chi
Park, Kyoung Sun
Do, Hackwon
Ae Kyung Park
Subject
Biochemistry & Molecular Biology
Keywords
Crystal structure; Leucosporidium sp.; X-ray crystallography; antifreeze protein; ice-binding protein
Issue Date
2012
Publisher
The American Society for Biochemistry and Molecular Biology
Citation
Kim, Hak Jun, et al. 2012. "Structural Basis for Antifreeze Activity of Ice-binding Protein from Arctic Yeast". JOURNAL OF BIOLOGICAL CHEMISTRY, 287(14): 11460-11468.
Abstract
Arctic yeast Leucosporidium sp. produces a glycosylated ice-binding protein (LeIBP) with a molecular mass of approximately 25 kDa, which can lower the freezing point below the melting point once it binds to ice. LeIBP is a member of a large class of ice-binding proteins, the structures of which are unknown. Here, we report the crystal structures of non-glycosylated LeIBP and glycosylated LeIBP at 1.57 ?and 2.43 ?resolution, respectively. Structural analysis of the LeIBPs revealed a dimeric right-handed β-helix fold, which is composed of three parts: a large coiled structural domain, a long helix region (residues 96?115 form a long α-helix that packs along one face of the β-helix) and a C-terminal hydrophobic loop region (243-PFVPAPEVV-251). Unexpectedly, the C- terminal hydrophobic loop region has an extended conformation pointing away from the body of the coiled structural domain and forms intertwined dimer interactions. In addition, structural analysis of glycosylated LeIBP with sugar moieties attached to Asn185 provides a basis for interpreting previous biochemical analyses as well as the increased stability and secretion of glycosylated LeIBP. We also determined that the aligned Thr/Ser/Ala residues are critical for ice binding within the B face of LeIBP using site-directed mutagenesis. Although LeIBP has a common β-helical fold similar to that of canonical harge class of ice-binding proteins, the structures of which are unknown. Here, we report the crystal structures of non-glycosylated LeIBP and glycosylated LeIBP at 1.57 ?and 2.43 ?resolution, respectively. Structural analysis of the LeIBPs revealed a dimeric right-handed β-helix fold, which is composed of three parts: a large coiled structural domain, a long helix region (residues 96?115 form a long α-helix that packs along one face of the β-helix) and a C-terminal hydrophobic loop region (243-PFVPAPEVV-251). Unexpected
URI
http://repository.kopri.re.kr/handle/201206/6364
DOI
http://dx.doi.org/10.1074/jbc.M111.331835
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