Determination of the Solution Structure of the N-Domain Plus Linker of Antarctic Eel Pout Antifreeze Protein RD3.
スポンサーリンク
概要
- 論文の詳細を見る
RD3, a new antifreeze protein (AFP) extracted from antarctic eel pout is a single polypeptide divided into homologous N-terminal (residues Asn1-Glu64) and C-terminal (residues Ser74-Glu134) domains, each of which has a high sequence identity with Type III AFP. A 9-residue linker (-D65GTTSPGLK73-) connects these two domains in tandem and is thought to play a significant role in defining the nature of the intact molecule. The present paper shows for the first time the solution structure and preliminary 15N-NMR backbone dynamics data of the N-domain plus the linker of recombinant RD3 protein (RD3-Nl: residues 1-73) by employing homo- and heteronuclear multidimensional NMR spectroscopy. Forty converged structures of RD3-N1 were successfully calculated by using a total of 958 NMR-derived structural restraints. It was found that the N-domain of RD3-N1 has a globular form comprising six β-strands, three type III turns, and several loops, which stabilize a flat, ice-binding site formed on one side of this domain. Further, the linker portion appears to have a definitive structure, which is independent of the globular N-domain. This definitive linker is roughly divided into two short strands, -D65GTTSP70-and-G71LK73-, which are bent around -T67TSPG71-at an angle of approximately 60°. This bending motif of the linker may function to orient the two ice-binding sites of the N-and C-domains of RD3 in the same direction, leading to their simultaneous interactions with the ice crystal surface.
- 社団法人 日本生化学会の論文
著者
-
Tsuda Sakae
Bioscience And Chemistry Division Division Hokkaido National Industrial Research Institute
-
Miura Kazunori
Division Of Biological Sciences Graduate School Of Science Hokkaido University
-
OHGIYA Satoru
Bioscience and Chemistry Division, Hokkaido National Industrial Research Institute (HNIRI)
-
NEMOTO Nobuaki
Varian Japan
-
ODAIRA Masato
Bioscience and Chemistry Division, Hokkaido National Industrial Research Institute (HNIRI)
-
Hoshino Tamotsu
Bioscience And Chemistry Division Hokkaido National Industrial Research Institute
-
Nitta Katsutoshi
Division Of Biological Sciences Graduate School Of Science Hokkaido University
-
Hoshino Tamotsu
Bioscience and Chemistry Division, Hokkaido National Industrial Research Institute (HNIRI)
関連論文
- A novel membrane-anchored cytochrome c-550 of alkaliphilic Bacillus clarkii K24-1U: expression, molecular features and properties of redox potential
- GENE CLONING OF THE FATTY ACID SYNTHASE FROM THE DHA PRODUCING PSYCHROPHILIC BACTERIUM, Vibrio marinus strain MP-1
- FREEZING RESISTANCE AMONG ISOLATES OF A PSYCHROPHILIC FUNGUS, TYPHULA ISHIKARIENSIS, FROM NORWAY (19th Symposium on Polar Biology)
- Isolation of Vibrio sp.S-1 Exhibiting Extraordinarily High Catalase Activity
- Cytochrome c-552 from Gram-Negative Alkaliphilic Pseudomonas alcaliphila AL15-21T Alters the Redox Properties at High pH
- Structural Analysis of an Antibacterial Peptide Derived from a Nematode
- Roles of Ser130 and Thr126 in Chloride Binding and Photocycle of pharaonis Halorhodopsin
- Side Chain-Side Chain Interactions of Arginine with Tyrosine and Aspartic Acid in Arg/Gly/Tyr-Rich Domains within Plant Glycine-Rich RNA Binding Proteins
- Ecological role of fungal infections of moss carpet in Svalbard (scientific paper)
- Identification of a Member of the Serralysin Family Isolated from a Psychrotrophic Bacterium, Pseudomonas fluorescens 114
- Solution Structure of an Insect Growth Factor Peptide GBP and its EGF Activity
- p-COUMARIC ACID FROM WHEAT INACTIVATES ICE-NUCLEATING ACTIVITY BY ICE-NUCLEATING BACTERIUM
- Secondary Structure and Ca^-Binding Property of the N-Terminal Half Domain of Calmodulin from Yeast Saccharomyces cerevisiae as Studied by NMR
- Determination of the Solution Structure of the N-Domain Plus Linker of Antarctic Eel Pout Antifreeze Protein RD3
- A filamentous fungus, Pythium ultimum TROW var. ultimum, isolated from moribund moss colonies from Svalbard, northern islands of Norway
- SEARCHING FOR NEW ANTIFREEZE SUBSTANCES FROM WHEAT
- Mutational Analysis of the Small Cytokine : Growth-Blocking Peptide (GBP) to Investigate the Interaction with Its Receptor in Insect Immune Cells
- The Volume and Compressibility Changes Associated with Protein Denaturation
- Cadmium-113 NMR Studies of Bovine and Human α-Lactalbumin and Equine Lysozyme
- Determination of the Solution Structure of the N-Domain Plus Linker of Antarctic Eel Pout Antifreeze Protein RD3.