Solution structure of the antifreeze-like domain of human sialic acid synthase.
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.
Hamada
Toshiyuki
T
RIKEN Genomic Sciences Center, Yokohama 230-0045, Japan.
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
D000595:Amino Acid Sequence; D021343:Antifreeze Proteins, Type III / Q000737:chemistry*; D019143:Evolution, Molecular; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D007652:Oxo-Acid-Lyases / Q000737:chemistry*; D010802:Phylogeny; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D012996:Solutions; D013329:Structure-Activity Relationship
D021343:Antifreeze Proteins, Type III; D012996:Solutions; C018730:N-acetylneuraminate synthase; D007652:Oxo-Acid-Lyases