6LEB

Staphylococcus aureus surface protein SdrC mutant-P366H

Summary for 6LEB

• Entry DOI: 10.2210/pdb6leb/pdb
• Descriptor: Ser-Asp rich fibrinogen-binding, bone sialoprotein-binding protein, MAGNESIUM ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: dimer, structural protein
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 71321.69

Authors

Hang, T.,Zhang, M.,Wang, J. (deposition date: 2019-11-25, release date: 2020-11-25, Last modification date: 2023-11-22)

Primary citation

Wang, J.,Zhang, M.,Wang, M.,Zang, J.,Zhang, X.,Hang, T.
Structural insights into the intermolecular interaction of the adhesin SdrC in the pathogenicity of Staphylococcus aureus.
Acta Crystallogr.,Sect.F, 77:47-53, 2021

PubMed Abstract: Staphylococcus aureus is an opportunistic disease-causing pathogen that is widely found in the community and on medical equipment. A series of virulence factors secreted by S. aureus can trigger severe diseases such as sepsis, endocarditis and toxic shock, and thus have a great impact on human health. The transformation of S. aureus from a colonization state to a pathogenic state during its life cycle is intimately associated with the initiation of bacterial aggregation and biofilm accumulation. SdrC, an S. aureus surface protein, can act as an adhesin to promote cell attachment and aggregation by an unknown mechanism. Here, structural studies demonstrate that SdrC forms a unique dimer through intermolecular interaction. It is proposed that the dimerization of SdrC enhances the efficiency of bacteria-host attachment and therefore contributes to the pathogenicity of S. aureus.

PubMed: 33620037
DOI: 10.1107/S2053230X21000741

Experimental method

X-RAY DIFFRACTION (1.54 Å)