2WY7

Staphylococcus aureus complement subversion protein Sbi-IV in complex with complement fragment C3d revealing an alternative binding mode

Summary for 2WY7

• Entry DOI: 10.2210/pdb2wy7/pdb
• Related: 1C3D 1GHQ 1W2S 2A73 2A74 2HR0 2WII 2WIN 2WY8
• Descriptor: COMPLEMENT C3D FRAGMENT, IGG-BINDING PROTEIN, GLYCEROL, ... (4 entities in total)
• Functional Keywords: immune system, immune response, innate immunity, complement pathway, inflammatory response
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Secreted: P01024
• Total number of polymer chains: 2
• Total formula weight: 44279.61

Authors

Clark, E.A.,Crennell, S.,Upadhyay, A.,Mackay, J.D.,Bagby, S.,van den Elsen, J.M. (deposition date: 2009-11-13, release date: 2010-12-01, Last modification date: 2024-10-23)

Primary citation

Clark, E.A.,Crennell, S.,Upadhyay, A.,Zozulya, A.V.,Mackay, J.D.,Svergun, D.I.,Bagby, S.,Van Den Elsen, J.M.
A Structural Basis for Staphylococcal Complement Subversion: X-Ray Structure of the Complement- Binding Domain of Staphylococcus Aureus Protein Sbi in Complex with Ligand C3D.
Mol.Immunol., 48:452-, 2011

PubMed Abstract: The structure of the complement-binding domain of Staphylococcus aureus protein Sbi (Sbi-IV) in complex with ligand C3d is presented. The 1.7Å resolution structure reveals the molecular details of the recognition of thioester-containing fragment C3d of the central complement component C3, involving interactions between residues of Sbi-IV helix α2 and the acidic concave surface of C3d. The complex provides a structural basis for the binding preference of Sbi for native C3 over C3b and explains how Sbi-IV inhibits the interaction between C3d and complement receptor 2. A second C3d binding site on Sbi-IV is identified in the crystal structure that is not observed in related S. aureus C3 inhibitors Efb-C and Ehp. This binding mode perhaps hints as to how Sbi-IV, as part of Sbi, forms a C3b-Sbi adduct and causes futile consumption of C3, an extraordinary aspect of Sbi function that is not shared by any other known Staphylococcal complement inhibitor.

PubMed: 21055811
DOI: 10.1016/J.MOLIMM.2010.09.017

Experimental method

X-RAY DIFFRACTION (1.7 Å)