2K5X

Chemical shift structure of COLICIN E9 DNASE domain with its cognate immunity protein IM9

Summary for 2K5X

• Entry DOI: 10.2210/pdb2k5x/pdb
• Related: 1emv 1fsj 1imq
• Descriptor: Colicin-E9 immunity protein, Colicin-E9 (2 entities in total)
• Functional Keywords: colicin e9, immunity protein im9, bacteriocin immunity, plasmid, antibiotic, antimicrobial, bacteriocin, endonuclease, hydrolase, metal-binding, nuclease, zinc, immune system-hydrolase complex, immune system/hydrolase
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 24712.52

Authors

Montalvao, R.W.,Cavalli, A.,Vendruscolo, M. (deposition date: 2008-07-01, release date: 2008-12-09, Last modification date: 2024-05-29)

Primary citation

Montalvao, R.W.,Cavalli, A.,Salvatella, X.,Blundell, T.L.,Vendruscolo, M.
Structure Determination of Protein-Protein Complexes Using NMR Chemical Shifts: Case of an Endonuclease Colicin-Immunity Protein Complex
J.Am.Chem.Soc., 130:15990-15996, 2008

PubMed Abstract: Nuclear magnetic resonance (NMR) spectroscopy provides a range of powerful techniques for determining the structures and the dynamics of proteins. The high-resolution determination of the structures of protein-protein complexes, however, is still a challenging problem for this approach, since it can normally provide only a limited amount of structural information at protein-protein interfaces. We present here the determination using NMR chemical shifts of the structure (PDB code 2K5X) of the cytotoxic endonuclease domain from bacterial toxin colicin (E9) in complex with its cognate immunity protein (Im9). In order to achieve this result, we introduce the CamDock method, which combines a flexible docking procedure with a refinement that exploits the structural information provided by chemical shifts. The results that we report thus indicate that chemical shifts can be used as structural restraints for the determination of the conformations of protein complexes that are difficult to obtain by more standard NMR approaches.

PubMed: 18980319

Experimental method

SOLUTION NMR