Crystal structure of human seminal diferric lactoferrin at 3.4 Angstrom resolution.
Lactoferrin was purified from human seminal fluid obtained from the semen bank. The purified samples were saturated with Fe3+ and crystallized by microdialysis method. The crystals belong to orthorhombic space group P21212, with a = 55.9 Angstrom. b = 97.2 Angstrom, c = 156.1 Angstrom and Z = 4. The structure was determined with molecular replacement method and refined to an R factor of 18.7% for all the data to 3.4 Angstrom resolution. The overall structure of seminal lactoferrin is similar to human colostrum lactoferrin. The amino acid sequence of seminal lactoferrin shows that it has one amino acid less than human colostrum lactoferrin and the structure of its N-terminal region is far more ordered than other lactoferrins. The structure of the iron-binding site and its immediate surroundings indicate well defined features.
Department of Biophysics, All India Institute of Medical Sciences, New Delhi 110029, India.
Janesh
J
Kumar
Wolfgang
W
Weber
Sabine
S
Münchau
Savita
S
Yadav
S Bhaskar
SB
Singh
K
K
Saravanan
M
M
Paramasivam
Sujata
S
Sharma
Punit
P
Kaur
A
A
Bhushan
A
A
Srinivasan
Christian
C
Betzel
T P
TP
Singh
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D006801:Humans; D007501:Iron / Q000378:metabolism*; D007781:Lactoferrin / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D012661:Semen / Q000201:enzymology*; D017421:Sequence Analysis
D007501:Iron; D007781:Lactoferrin