5MKC

Crystal structure of the RrgA Jo.In complex

Summary for 5MKC

• Entry DOI: 10.2210/pdb5mkc/pdb
• Descriptor: Cell wall surface anchor family protein (Jo),Cell wall surface anchor family protein (In), SULFATE ION, NICKEL (II) ION, ... (5 entities in total)
• Functional Keywords: bacteria, peptidoglycan, pilus adhesin, cross-links, folding, post-translational, isopeptide bond, biotechnology, cell adhesion
• Biological source: Streptococcus pneumoniae; More
• Total number of polymer chains: 6
• Total formula weight: 158575.82

Authors

Bonnet, J.,Cartannaz, J.,Tourcier, G.,Contreras-Martel, C.,Kleman, J.P.,Fenel, D.,Schoehn, G.,Morlot, C.,Vernet, T.,Di Guilmi, A.M. (deposition date: 2016-12-03, release date: 2017-03-15, Last modification date: 2024-10-16)

Primary citation

Bonnet, J.,Cartannaz, J.,Tourcier, G.,Contreras-Martel, C.,Kleman, J.P.,Morlot, C.,Vernet, T.,Di Guilmi, A.M.
Autocatalytic association of proteins by covalent bond formation: a Bio Molecular Welding toolbox derived from a bacterial adhesin.
Sci Rep, 7:43564-43564, 2017

PubMed Abstract: Unusual intramolecular cross-links present in adhesins from Gram-positive bacteria have been used to develop a generic process amenable to biotechnology applications. Based on the crystal structure of RrgA, the Streptococcus pneumoniae pilus adhesin, we provide evidence that two engineered protein fragments retain their ability to associate covalently with high specificity, in vivo and in vitro, once isolated from the parent protein. We determined the optimal conditions for the assembly of the complex and we solved its crystal structure at 2 Å. Furthermore, we demonstrate biotechnological applications related to antibody production, nanoassembly and cell-surface labeling based on this process we named Bio Molecular Welding.

PubMed: 28252635
DOI: 10.1038/srep43564

Experimental method

X-RAY DIFFRACTION (2.04 Å)