Crystal Structure of Human BPI and Two Bound Phospholipids at 2.4 Angstrom Resolution

Bactericidal/permeability-increasing protein (BPI), a potent antimicrobial protein of 456 residues, binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria. At a resolution of 2.4 angstroms, the crystal structure of human BPI shows a boomerang-shaped molecule f...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1997-06, Vol.276 (5320), p.1861-1864
Main Authors: Beamer, Lesa J., Carroll, Stephen F., Eisenberg, David
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Analytical, structural and metabolic biochemistry
Antibacterial agents
Antimicrobial Cationic Peptides
Atoms
Bacteria
Binding and carrier proteins
Binding Sites
Biological and medical sciences
Blood Bactericidal Activity
Blood Proteins - chemistry
Blood Proteins - metabolism
Crystal structure
Crystallization
Crystallography, X-Ray
Crystals
Datasets
Disulfides
Electron density
Endotoxins
Fundamental and applied biological sciences. Psychology
Humans
Infections
Lipids
Lipopolysaccharides - metabolism
Medical research
Membrane Proteins
Models, Molecular
Molecular Sequence Data
Molecules
Phosphatidylcholines - chemistry
Phosphatidylcholines - metabolism
Phospholipids
Physiological aspects
Protein Conformation
Protein structure
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Scientific Concepts
Structural Elements (Construction)
Structure
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Summary:Bactericidal/permeability-increasing protein (BPI), a potent antimicrobial protein of 456 residues, binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria. At a resolution of 2.4 angstroms, the crystal structure of human BPI shows a boomerang-shaped molecule formed by two similar domains. Two apolar pockets on the concave surface of the boomerang each bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide. As a model for the related plasma lipid transfer proteins, BPI illuminates a mechanism of lipid transfer for this protein family.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.276.5320.1861