3UJP
Structure of MntC protein at 2.7A
Summary for 3UJP
| Entry DOI | 10.2210/pdb3ujp/pdb |
| Descriptor | Mn transporter subunit, MANGANESE (II) ION, ZINC ION, ... (5 entities in total) |
| Functional Keywords | manganese binding protein, metal binding protein |
| Biological source | Synechocystis sp. PCC 6803 |
| Total number of polymer chains | 3 |
| Total formula weight | 102431.83 |
| Authors | Kanteev, M.,Adir, N. (deposition date: 2011-11-08, release date: 2012-11-14, 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 Cited by 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: 23519795DOI: 10.1107/S174430911300153X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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