Amino acid sequence and crystal structure of buffalo alpha-lactalbumin.
Isolation, purification, amino acid sequence determination and X-ray crystal structure of buffalo alpha-lactalbumin were performed in order to gain further knowledge of the molecular basis of alpha-lactalbumin in the lactose synthase complex. The deduced amino acid sequence differs at one position from the bovine alpha-lactalbumin sequence (at position 17). The refined crystal structure at 2.3 A is very similar to those previously reported for human and baboon alpha-lactalbumins. However, a portion of the molecule (residues 105-109) exhibits different conformation. It forms a 'flexible loop', and appears to be a functionally important region in forming the lactose synthase complex.
Calderone
V
V
School of Biology and Biochemistry, University of Bath, UK.
Giuffrida
M G
MG
Viterbo
D
D
Napolitano
L
L
Fortunato
D
D
Conti
A
A
Acharya
K R
KR
D000595:Amino Acid Sequence; D000818:Animals; D002020:Buffaloes; D002845:Chromatography; D018360:Crystallography, X-Ray; D007768:Lactalbumin / Q000737:chemistry* / Q000302:isolation & purification; D013058:Mass Spectrometry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
D007768:Lactalbumin