Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 69, Part 3 (March 2013)


structural communications



Acta Cryst. (2013). F69, 237-242    [ doi:10.1107/S174430911300153X ]

Arginine 116 stabilizes the entrance to the metal ion-binding site of the MntC protein

M. Kanteev and N. Adir

Abstract: The cyanobacterium Synechocystis sp. PCC 6803 imports Mn2+ ions via MntCAB, an ABC transport system that is expressed at submicromolar Mn2+ concentrations. The structures of the wild type (WT) and a site-directed mutant of the MntC solute-binding protein have been determined at 2.7 and 3.5 Å resolution, respectively. The WT structure is significantly improved over the previously determined structure (PDB entry 1xvl), showing improved Mn2+ binding site parameters, disulfide bonds in all three monomers and ions bound to the protein surface, revealing the role of Zn2+ ions in the crystallization liquor. The structure of MntC reveals that the active site is surrounded by neutral-to-positive electrostatic potential and is dominated by a network of polar interactions centred around Arg116. The mutation of this residue to alanine was shown to destabilize loops in the entrance to the metal-ion binding site and suggests a possible role in MntC function.

PDB references: 3ujp and 3v63

Keywords: ABC transporter; site-directed mutagenesis; cyanobacteria.


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