351. Solution structure of the antifreeze-like domain of human sialic acid synthase.
- Author
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Hamada T, Ito Y, Abe T, Hayashi F, Güntert P, Inoue M, Kigawa T, Terada T, Shirouzu M, Yoshida M, Tanaka A, Sugano S, Yokoyama S, and Hirota H
- Subjects
- Amino Acid Sequence, Evolution, Molecular, Humans, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Conformation, Sequence Homology, Amino Acid, Solutions, Structure-Activity Relationship, Antifreeze Proteins, Type III chemistry, Oxo-Acid-Lyases chemistry
- Abstract
The structure of the C-terminal antifreeze-like (AFL) domain of human sialic acid synthase was determined by NMR spectroscopy. The structure comprises one alpha- and two single-turn 3(10)-helices and two beta-strands, and is similar to those of the type III antifreeze proteins. Evolutionary trace analyses of the type III antifreeze protein family suggested that the class-specific residues in the human and bacterial AFL domains are important for their substrate binding, while the class-specific residues of the fish antifreeze proteins are gathered on the ice-binding surface.
- Published
- 2006
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