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. 2011 Jul 22;108(33):E480-E487. doi: 10.1073/pnas.1103367108

Fig. 6.

Fig. 6.

Effect of conserved MamA residue mutation. (A) Superposition of native MamAΔ41 (green) and MamAΔ41 R50E (NTD- yellow, CTD- red) reveals a large rotation of the mutant NTD. Highly conserved residues Arg50 and Asp 159 form a salt bridge connecting TPR1 and TPR2 (light pink) in the wild type structure. (B) Side and top views of representative symmetry-related monomers demonstrate the superhelical crystal packing of MamAΔ41 R50E. The continuous superhelix is formed by the CTD (light gray) of each monomer, while adjacent NTDs (dark gray) lie perpendicular to the superhelix long axis. A single representative monomer in this packing is highlighted (NTD- yellow, CTD- red) (C) Superposition of native MamAΔ41 (brown) and MamAΔ41 D159K (light pink) reveals no major structural differences caused by this point mutation. (D) Size exclusion (Superdex 200) chromatograms of wild type MamA and mutants demonstrating alterations in the MamA oligomeric state. Full-length wild type M. magneticum MamA, M. gryphiswaldense MamA and MamA D159K (blue, pink, and orange respectively) eluted at a volume corresponding to ∼500 kDa. Full-length MamA R50E mutant eluted at volumes appropriate for the dimer and monomer. The MamAΔ41 mutant (red) eluted at a volume appropriate for a monomer.