1ucs

Type III Antifreeze Protein RD1 from an Antarctic Eel Pout

spinqualitylabelsall models 1ucs, resolution 0.62Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ucs is a 1 chain structure with sequence from Lycodichthys dearborni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1msi, 1hg7, 1ops Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ANP1_RHIDE] Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point. Binds to nascent ice crystals and prevents further growth (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed RD1 is a 7-kDa globular protein from the Antarctic eel pout Lycodichthys dearborni. It belongs to type III of the four types of antifreeze proteins (AFPs) found in marine fishes living at subzero temperatures. For type III AFP, a potential ice-binding flat surface has been identified and is imbedded with side chains capable of making hydrogen bonds with a specific lattice plane on ice. So far, all crystallographic studies on type III AFPs were carried out using the Atlantic ocean pout Macrozoarces americanus as the source organism. Here we present the crystal structure of a type III AFP from a different zoarcid fish, and at an ultra-high resolution of 0.62 A. The protein fold of RD1 comprises a compact globular domain with two internal tandem motifs arranged about a pseudo-dyad symmetry. Each motif of the "pretzel fold" includes four short beta-strands and a 3(10) helix. There is a novel internal cavity of 45 A(3) surrounded by eight conserved nonpolar residues. The model contains several residues with alternate conformations, and a number of split water molecules, probably caused by alternate interactions with the protein molecule. After extensive refinement that includes hydrogen atoms, significant residual electron densities associated with the electrons of peptides and many other bonds could be visualized. The refined crystal structure of an eel pout type III antifreeze protein RD1 at 0.62-A resolution reveals structural microheterogeneity of protein and solvation.,Ko TP, Robinson H, Gao YG, Cheng CH, DeVries AL, Wang AH Biophys J. 2003 Feb;84(2 Pt 1):1228-37. PMID:12547803 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Antifreeze protein

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