3V10

Crystal structure of the collagen binding domain of Erysipelothrix rhusiopathiae surface protein RspB

Summary for 3V10

• Entry DOI: 10.2210/pdb3v10/pdb
• Related: 2f6a 2z1p
• Descriptor: Rhusiopathiae surface protein B (2 entities in total)
• Functional Keywords: rhusiopathiae surface protein b, collagen hug model, dev-igg fold, collagen binding protein, cell adhesion
• Biological source: Erysipelothrix rhusiopathiae
• Total number of polymer chains: 2
• Total formula weight: 71401.75

Authors

Ponnuraj, K.,Swarmistha devi, A.,Ogawa, Y.,Shimoji, Y.,Subramainan, B. (deposition date: 2011-12-09, release date: 2012-10-24, Last modification date: 2024-03-20)

Primary citation

Devi, A.S.,Ogawa, Y.,Shimoji, Y.,Balakumar, S.,Ponnuraj, K.
Collagen adhesin-nanoparticle interaction impairs adhesin's ligand binding mechanism
Biochim.Biophys.Acta, 1820:819-828, 2012

PubMed Abstract: Pathogenic bacteria specifically recognize extracellular matrix (ECM) molecules of the host (e.g. collagen, fibrinogen and fibronectin) through their surface proteins known as MSCRAMMs (Microbial Surface Components Recognizing Adhesive Matrix Molecules) and initiate colonization. On implantation, biomaterials easily get coated with these ECM molecules and the MSCRAMMs mediate bacterial adherence to biomaterials. With the rapid rise in antibiotic resistance, designing alternative strategies to reduce/eliminate bacterial colonization is absolutely essential.

PubMed: 22538248
DOI: 10.1016/j.bbagen.2012.04.006

Experimental method

X-RAY DIFFRACTION (1.75 Å)