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Solution structure of the antifreeze‐like domain of human sialic acid synthase
Author(s) -
Hamada Toshiyuki,
Ito Yoko,
Abe Takamasa,
Hayashi Fumiaki,
Güntert Peter,
Inoue Makoto,
Kigawa Takanori,
Terada Takaho,
Shirouzu Mikako,
Yoshida Mayumi,
Tanaka Akiko,
Sugano Sumio,
Yokoyama Shigeyuki,
Hirota Hiroshi
Publication year - 2006
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.051700406
Subject(s) - antifreeze protein , antifreeze , biochemistry , chemistry , sialic acid , psychrophile , amino acid , enzyme , stereochemistry , biophysics , biology , organic chemistry
The structure of the C‐terminal antifreeze‐like (AFL) domain of human sialic acid synthase was determined by NMR spectroscopy. The structure comprises one α‐ and two single‐turn 3 10 ‐helices and two β‐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.