4IRM

Crystal structure of mntc r116a mutant exhibits flexibility in the c-terminal domain

Replaces:  3V63

Summary for 4IRM

• Entry DOI: 10.2210/pdb4irm/pdb
• Related: 1XVL 3UJP
• Descriptor: Mn transporter; MntC, MANGANESE (II) ION (2 entities in total)
• Functional Keywords: manganese, transport protein, solute binding protein of abs transporter
• Biological source: Synechocystis sp.
• Total number of polymer chains: 3
• Total formula weight: 108207.21

Authors

Kanteev, M.,Adir, N. (deposition date: 2013-01-15, release date: 2013-02-06, Last modification date: 2024-11-20)

Primary citation

Kanteev, M.,Adir, N.
Arginine 116 stabilizes the entrance to the metal ion-binding site of the MntC protein.
Acta Crystallogr.,Sect.F, 69:237-242, 2013

PubMed 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.

PubMed: 23519795
DOI: 10.1107/S174430911300153X

Experimental method

X-RAY DIFFRACTION (3.5 Å)