2GOX

Crystal structure of Efb-C / C3d Complex

Summary for 2GOX

• Entry DOI: 10.2210/pdb2gox/pdb
• Related: 2GOM 2NOJ
• Descriptor: Complement C3, Fibrinogen-binding protein (3 entities in total)
• Functional Keywords: protein-protein complex, cell adhesion-toxin complex, cell adhesion/toxin
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P01024 P68799
• Total number of polymer chains: 4
• Total formula weight: 81473.56

Authors

Hammel, M.,Geisbrecht, B.V. (deposition date: 2006-04-14, release date: 2007-03-20, Last modification date: 2024-11-06)

Primary citation

Hammel, M.,Sfyroera, G.,Ricklin, D.,Magotti, P.,Lambris, J.D.,Geisbrecht, B.V.
A structural basis for complement inhibition by Staphylococcus aureus.
Nat.Immunol., 8:430-437, 2007

PubMed Abstract: 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.

PubMed: 17351618
DOI: 10.1038/ni1450

Experimental method

X-RAY DIFFRACTION (2.2 Å)