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Structural basis for the Antifreeze activity of an Ice Binding Protein (LeIBP) from Arctic yeast

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dc.contributor.authorPark, Kyoung Sun-
dc.contributor.authorKim, Eunjung-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorKang, Sung-Ho-
dc.contributor.authorKim, Hak Jun-
dc.contributor.authorLee, Sung Gu-
dc.contributor.authorPark, Jong-chan-
dc.contributor.authorDo, Hackwon-
dc.date.accessioned2018-04-05T15:12:23Z-
dc.date.accessioned2018-04-05T15:12:23Z-
dc.date.available2018-04-05T15:12:23Z-
dc.date.available2018-04-05T15:12:23Z-
dc.date.issued2011-
dc.identifier.urihttp://repository.kopri.re.kr/handle/201206/8471-
dc.description.abstractPsychrophilic Arctic yeast, Leucosporidium sp. produces a glyco-ice binding protein (LeIBP) with a molecular mass of about 25 kDa that has a unique ability to lower the freezing point below the melting point once it binds to ice. Antifreeze proteins (AFPs) and ice binding proteins (IBPs) are found in many polar organisms and inhibit the growth of ice crystals to protect themselves from freezing. LeIBP exhibits the least protein sequence similarity with other previous known antifreeze protein structures. To better understand the ice binding mechanism of LeIBP, we have expressed full-length recombinant LeIBP in large amounts in Escherichia coli and purified the proteins. Here, we report the crystal structure of LeIBP at 1.57 Å resolution. Structural analysis of LeIBP 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 which 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 an intertwined dimer interactions. From this structure we propose an ice binding sites, which is flat and contains a regular pattern of aligned Thr, Ala and Ser residues. Furthermore, we su-
dc.language영어-
dc.titleStructural basis for the Antifreeze activity of an Ice Binding Protein (LeIBP) from Arctic yeast-
dc.title.alternative북극효모유래 결빙방지단백질의 고해상도 삼차 구조연구-
dc.typeProceeding-
dc.identifier.bibliographicCitationPark, Kyoung Sun, et al. 2011. Structural basis for the Antifreeze activity of an Ice Binding Protein (LeIBP) from Arctic yeast. 한국생물공학회. 한국생물공학회. 2011.12.12~.-
dc.citation.volume1-
dc.citation.number1-
dc.citation.conferenceDate2011.12.12~-
dc.citation.conferenceName한국생물공학회-
dc.citation.conferencePlace한국생물공학회-
dc.description.articleClassificationPro(초록)국내-
dc.subject.keywordAntifreeze protein-
dc.subject.keywordArctic yeast-
dc.subject.keywordCrystal structure-
dc.subject.keywordLeucosporidium sp.-
dc.subject.keywordice binding protein-
dc.identifier.localId2011-0341-
Appears in Collections  
2011-2012, Developing cryoprotectant materials derived from antifreeze proteins for the cryopreservation of valuable bioresources (11-12) / Kim, Hak Jun
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