2gom
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Crystal structure of Efb-C from Staphylococcus aureus
OverviewOverview
To provide insight into bacterial suppression of complement-mediated, immunity, we present here structures of a bacterial complement inhibitory, protein, both free and bound to its complement target. The 1.25-A, structure of the complement component C3-inhibitory domain of, Staphylococcus aureus extracellular fibrinogen-binding protein (Efb-C), demonstrated a helical motif involved in complement regulation, whereas, the 2.2-A structure of Efb-C bound to the C3d domain of human C3 allowed, insight into the recognition of complement proteins by invading pathogens., Our structure-function studies provided evidence for a previously, unrecognized mode of complement inhibition whereby Efb-C binds to native, C3 and alters the solution conformation of C3 in a way that renders it, unable to participate in successful 'downstream' activation of the, complement response.
About this StructureAbout this Structure
2GOM is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
A structural basis for complement inhibition by Staphylococcus aureus., Hammel M, Sfyroera G, Ricklin D, Magotti P, Lambris JD, Geisbrecht BV, Nat Immunol. 2007 Apr;8(4):430-437. Epub 2007 Mar 11. PMID:17351618
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