2KXO

Solution NMR structure of the cell division regulator MinE protein from Neisseria gonorrhoeae

Summary for 2KXO

• Entry DOI: 10.2210/pdb2kxo/pdb
• Descriptor: Cell division topological specificity factor (1 entity in total)
• Functional Keywords: mine, cell division, neisseria gonorrhoeae, mind-binding, topological specificity, cell cycle
• Biological source: Neisseria gonorrhoeae
• Total number of polymer chains: 2
• Total formula weight: 22133.54

Authors

Ghasriani, H.,Goto, N.K.,Ducat, T. (deposition date: 2010-05-11, release date: 2010-10-20, Last modification date: 2024-05-01)

Primary citation

Ghasriani, H.,Ducat, T.,Hart, C.T.,Hafizi, F.,Chang, N.,Al-Baldawi, A.,Ayed, S.H.,Lundstrom, P.,Dillon, J.A.,Goto, N.K.
Appropriation of the MinD protein-interaction motif by the dimeric interface of the bacterial cell division regulator MinE.
Proc.Natl.Acad.Sci.USA, 107:18416-18421, 2010

PubMed Abstract: MinE is required for the dynamic oscillation of Min proteins that restricts formation of the cytokinetic septum to the midpoint of the cell in gram negative bacteria. Critical for this oscillation is MinD-binding by MinE to stimulate MinD ATP hydrolysis, a function that had been assigned to the first ∼30 residues in MinE. Previous models based on the structure of an autonomously folded dimeric C-terminal fragment suggested that the N-terminal domain is freely accessible for interactions with MinD. We report here the solution NMR structure of the full-length MinE dimer from Neisseria gonorrhoeae, with two parts of the N-terminal domain forming an integral part of the dimerization interface. Unexpectedly, solvent accessibility is highly restricted for residues that were previously hypothesized to directly interact with MinD. To delineate the true MinD-binding region, in vitro assays for MinE-stimulated MinD activity were performed. The relative MinD-binding affinities obtained for full-length and N-terminal peptides from MinE demonstrated that residues that are buried in the dimeric interface nonetheless participate in direct interactions with MinD. According to results from NMR spin relaxation experiments, access to these buried residues may be facilitated by the presence of conformational exchange. We suggest that this concealment of MinD-binding residues by the MinE dimeric interface provides a mechanism for prevention of nonspecific interactions, particularly with the lipid membrane, to allow the free diffusion of MinE that is critical for Min protein oscillation.

PubMed: 20937912
DOI: 10.1073/pnas.1007141107

Experimental method

SOLUTION NMR