1VFE

HUMAN LACTOFERRIN, N-TERMINAL LOBE MUTANT WITH ARG 121 REPLACED BY SER (R121S)

1VFE の概要

• エントリーDOI: 10.2210/pdb1vfe/pdb
• 分子名称: HUMAN LACTOFERRIN, FE (III) ION, CARBONATE ION, ... (4 entities in total)
• 機能のキーワード: transferrin, iron transport, glycoprotein, metal-binding, recombinant half molecule, mutant
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Isoform 1: Secreted. Isoform DeltaLf: Cytoplasm: P02788
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37066.77

構造登録者

Faber, H.R.,Day, C.L.,Baker, E.N. (登録日: 1996-10-01, 公開日: 1997-04-01, 最終更新日: 2024-10-16)

主引用文献

Faber, H.R.,Baker, C.J.,Day, C.L.,Tweedie, J.W.,Baker, E.N.
Mutation of arginine 121 in lactoferrin destabilizes iron binding by disruption of anion binding: crystal structures of R121S and R121E mutants.
Biochemistry, 35:14473-14479, 1996

PubMed Abstract: A conserved arginine residue helps to form the synergistic anion binding site in transferrins. To probe the importance of this residue for anion binding and iron binding, Arg 121 has been mutated to Ser and Glu in N-terminal half-molecule of human lactoferrin. The two mutants, R121S and R121E, have been expressed, purified, and crystallized. Their three-dimensional structures have been determined by X-ray diffraction at 2.3 and 2.5 A resolution, respectively. The structures were determined by molecular replacement and were refined by restrained least squares methods to final R values of 0.185 and 0.204. Both mutants still bind iron but with decreased stability. The crystal structures show that destabilization of iron binding probably results from disruption of the anion binding site; mutation of Arg 121 removes one wall of the anion binding pocket and causes the synergistic carbonate ion to be displaced 0.5 A from its position in the wild-type protein. In the process it becomes partially detached from the helix N-terminus that forms the rest of the anion binding site.

PubMed: 8931543
DOI: 10.1021/bi961729g

実験手法

X-RAY DIFFRACTION (2.3 Å)