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Solution structure of the antifreeze-like domain of human sialic acid synthase.

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.

SUBMITTER: Hamada T

PROVIDER: S-EPMC2242509 | biostudies-literature | 2006 May

REPOSITORIES: biostudies-literature

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Solution structure of the antifreeze-like domain of human sialic acid synthase.

Hamada Toshiyuki T Ito Yoko Y Abe Takamasa T Hayashi Fumiaki F Güntert Peter P Inoue Makoto M Kigawa Takanori T Terada Takaho T Shirouzu Mikako M Yoshida Mayumi M Tanaka Akiko A Sugano Sumio S Yokoyama Shigeyuki S Hirota Hiroshi H

Protein science : a publication of the Protein Society 20060405 5

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 r ...[more]

PMID: 16597820

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