Structural and functional analogy between pneumolysin and proaerolysin.
Pneumolysin and proaerolysin are bacterial toxins that form pores in host cells by oligomerization. We propose that they may have similar structures despite a poor sequence identity. The crystal structure of proaerolysin reveals a protein composed of four domains, arranged in the shape of an elongated comma. Electron microscopy of the pneumolysin monomer shows a similar arrangement of domains. The sequence of pneumolysin recognizes the template of proaerolysin from a library of protein folds. A three-dimensional model of pneumolysin has been constructed by the comparative approach using the structure of proaerolysin. This model, together with results on the activity of site-specific mutants and the positions of antigenic sites, has been used to propose functional roles of individual domains.
Sowdhamini
R
R
Imperial Cancer Research Fund, Unit of Structural Molecular Biology, Department of Crystallography, Birkbeck College, UK.
Mitchell
T J
TJ
Andrew
P W
PW
Morgan
P J
PJ
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001427:Bacterial Toxins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006460:Hemolysin Proteins / Q000737:chemistry; D008854:Microscopy, Electron; D008958:Models, Molecular; D008969:Molecular Sequence Data; D052899:Pore Forming Cytotoxic Proteins; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D012984:Software; D013301:Streptolysins / Q000737:chemistry*; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D001427:Bacterial Toxins; D006460:Hemolysin Proteins; D052899:Pore Forming Cytotoxic Proteins; D013301:Streptolysins; C032290:plY protein, Streptococcus pneumoniae; C107096:proaerolysin; C032676:aerolysin