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Structural characterization of the α‐hemolysin monomer from Staphylococcus aureus
Author(s) -
Meesters Christian,
Brack Antje,
Hellmann Nadja,
Decker Heinz
Publication year - 2009
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22227
Subject(s) - monomer , hemolysin , lysis , staphylococcus aureus , chemistry , membrane , crystallography , biophysics , materials science , bacteria , biochemistry , polymer , biology , organic chemistry , genetics , virulence , gene
α‐Hemolysin from Staphylococcus aureus is secreted as a water‐soluble monomer and assembles on membranes to oligomerize into a homo‐heptameric, water‐filled pore. These pores lead to lysis and cell death. Although the structure of the heptameric pore is solved by means of X‐ray crystallography, structures of intermediate states—from the soluble monomer to all potential “pre‐pore” structures—are yet unknown. Here, we propose a model of the monomeric α‐hemolysin in solution based on molecular modeling, verified by small angle X‐ray scattering data. This structure reveals details of the monomeric conformation of the α‐hemolysin, for example inherent flexibility, along with definite differences in comparison to the structures used as templates. Proteins 2009. © 2008 Wiley‐Liss, Inc.