دورية أكاديمية

Structure of a bacterial ice binding protein with two faces of interaction with ice

التفاصيل البيبلوغرافية
العنوان: Structure of a bacterial ice binding protein with two faces of interaction with ice
المؤلفون: Mangiagalli, M, Sarusi, G, Kaleda, A, Bar Dolev, M, Nardone, V, Vena, VF, Braslavsky, I, Lotti, M, Nardini, M
المساهمون: Mangiagalli, M, Sarusi, G, Kaleda, A, Bar Dolev, M, Nardone, V, Vena, V, Braslavsky, I, Lotti, M, Nardini, M
بيانات النشر: Blackwell Publishing Ltd
سنة النشر: 2018
المجموعة: Università degli Studi di Milano-Bicocca: BOA (Bicocca Open Archive)
مصطلحات موضوعية: Cold adaptation, DUF3494, IBP-1 fold, Ice recrystallization inhibition, Thermal hysteresi, Biochemistry, Molecular Biology, Cell Biology, BIO/10 - BIOCHIMICA, FIS/07 - FISICA APPLICATA (A BENI CULTURALI, AMBIENTALI, BIOLOGIA E MEDICINA)
الوصف: Ice-binding proteins (IBPs) contribute to the survival of many living beings at subzero temperature by controlling the formation and growth of ice crystals. This work investigates the structural basis of the ice-binding properties of EfcIBP, obtained from Antarctic bacteria. EfcIBP is endowed with a unique combination of thermal hysteresis and ice recrystallization inhibition activity. The three-dimensional structure, solved at 0.84 Å resolution, shows that EfcIBP belongs to the IBP-1 fold family, and is organized in a right-handed β-solenoid with a triangular cross-section that forms three protein surfaces, named A, B, and C faces. However, EfcIBP diverges from other IBP-1 fold proteins in relevant structural features including the lack of a 'capping' region on top of the β-solenoid, and in the sequence and organization of the regions exposed to ice that, in EfcIBP, reveal the presence of threonine-rich ice-binding motifs. Docking experiments and site-directed mutagenesis pinpoint that EfcIBP binds ice crystals not only via its B face, as common to other IBPs, but also via ice-binding sites on the C face. Database: Coordinates and structure factors have been deposited in the Protein Data Bank under accession number 6EIO
نوع الوثيقة: article in journal/newspaper
اللغة: English
العلاقة: info:eu-repo/semantics/altIdentifier/pmid/29533528; info:eu-repo/semantics/altIdentifier/wos/WOS:000431678400008; volume:285; issue:9; firstpage:1653; lastpage:1666; numberofpages:14; journal:THE FEBS JOURNAL; http://hdl.handle.net/10281/196942Test; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85044920072; http://onlinelibrary.wiley.com/journal/10.1111Test/(ISSN)1742-4658
DOI: 10.1111/febs.14434
DOI: 10.1111/(ISSN)1742-4658
الإتاحة: https://doi.org/10.1111/febs.14434Test
http://hdl.handle.net/10281/196942Test
حقوق: info:eu-repo/semantics/closedAccess
رقم الانضمام: edsbas.2E4EE350
قاعدة البيانات: BASE