2OFQ

NMR Solution Structure of a complex between the VirB9/VirB7 interaction domains of the pKM101 type IV secretion system

Summary for 2OFQ

• Entry DOI: 10.2210/pdb2ofq/pdb
• Descriptor: TraO, TraN (2 entities in total)
• Functional Keywords: trao, tran, pkm101, protein transport-protein transport complex, protein transport/protein transport
• Biological source: IncN plasmid R46; More
• Total number of polymer chains: 2
• Total formula weight: 13382.97

Authors

Harris, R.,Bayliss, R.,Driscoll, P.C.,Waksman, G. (deposition date: 2007-01-04, release date: 2007-01-23, Last modification date: 2023-12-27)

Primary citation

Bayliss, R.,Harris, R.,Coutte, L.,Monier, A.,Fronzes, R.,Christie, P.J.,Driscoll, P.C.,Waksman, G.
NMR structure of a complex between the VirB9/VirB7 interaction domains of the pKM101 type IV secretion system
Proc.Natl.Acad.Sci.Usa, 104:1673-1678, 2007

PubMed Abstract: Type IV secretion (T4S) systems translocate DNA and protein effectors through the double membrane of Gram-negative bacteria. The paradigmatic T4S system in Agrobacterium tumefaciens is assembled from 11 VirB subunits and VirD4. Two subunits, VirB9 and VirB7, form an important stabilizing complex in the outer membrane. We describe here the NMR structure of a complex between the C-terminal domain of the VirB9 homolog TraO (TraO(CT)), bound to VirB7-like TraN from plasmid pKM101. TraO(CT) forms a beta-sandwich around which TraN winds. Structure-based mutations in VirB7 and VirB9 of A. tumefaciens show that the heterodimer interface is conserved. Opposite this interface, the TraO structure shows a protruding three-stranded beta-appendage, and here, we supply evidence that the corresponding region of VirB9 of A. tumefaciens inserts in the membrane and protrudes extracellularly. This complex structure elucidates the molecular basis for the interaction between two essential components of a T4S system.

PubMed: 17244707
DOI: 10.1073/pnas.0609535104

Experimental method

SOLUTION NMR