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Published online before print April 5, 2006, 10.1110/ps.051700406
Protein Science (2006), 15:1010-1016. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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Solution structure of the antifreeze-like domain of human sialic acid synthase

Toshiyuki Hamada1,2,6, Yoko Ito2,6, Takamasa Abe1, Fumiaki Hayashi1, Peter Güntert1, Makoto Inoue1, Takanori Kigawa1, Takaho Terada1, Mikako Shirouzu1, Mayumi Yoshida1, Akiko Tanaka1, Sumio Sugano3, Shigeyuki Yokoyama1,4,5 and Hiroshi Hirota1,2

1 RIKEN Genomic Sciences Center, Yokohama 230-0045, Japan
2 Division of Protein Folds Research, Graduate School of Yokohama City University, Yokohama 230-0045, Japan
3 Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Tokyo 108-8639, Japan
4 RIKEN SPring-8 Center, Harima Institute, Hyogo 679-5148, Japan
5 Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan

(RECEIVED July 16, 2005; FINAL REVISION February 5, 2006; ACCEPTED February 12, 2006)

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 310-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.

Keywords: NMR; protein structure; antifreeze-like domain; sialic acid synthase; structural genomics


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