2gom

Crystal structure of Efb-C from Staphylococcus aureusCrystal structure of Efb-C from Staphylococcus aureus

Structural highlights 2gom is a 2 chain structure with sequence from Staphylococcus aureus subsp. aureus Mu50. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FIB_STAAM Binds to host fibrinogen (By similarity). Publication Abstract from PubMed 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. 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):430-7. Epub 2007 Mar 11. PMID:17351618 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Fibrinogen binding protein

spinqualitylabelsall models 2gom, resolution 1.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image