4K3I
Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of MauG, C2 Space Group
Summary for 4K3I
| Entry DOI | 10.2210/pdb4k3i/pdb |
| Related | 3SXT |
| Descriptor | Methylamine utilization protein MauG, Methylamine dehydrogenase light chain, Methylamine dehydrogenase heavy chain, ... (9 entities in total) |
| Functional Keywords | oxidoreductase |
| Biological source | Paracoccus denitrificans More |
| Cellular location | Periplasm: Q51658 P22619 |
| Total number of polymer chains | 6 |
| Total formula weight | 199972.19 |
| Authors | Yukl, E.Y.,Wilmot, C.M. (deposition date: 2013-04-10, release date: 2013-07-10, Last modification date: 2023-12-06) |
| Primary citation | Yukl, E.T.,Jensen, L.M.,Davidson, V.L.,Wilmot, C.M. Structures of MauG in complex with quinol and quinone MADH. Acta Crystallogr.,Sect.F, 69:738-743, 2013 Cited by PubMed Abstract: MauG has been cocrystallized with methylamine dehydrogenase (MADH) with its TTQ cofactor in the o-quinol (TTQOQ) and quinone (TTQOX) forms and the structures of the resulting complexes have been solved. The TTQOQ structure crystallized in either space group P21 or C2, while the TTQOX structure crystallized in space group P1. The previously solved structure of MauG in complex with MADH bearing an incompletely formed TTQ cofactor (preMADH) also crystallized in space group P1, although with different unit-cell parameters. Despite the changes in crystal form, the structures are virtually identical, with only very minor changes at the protein-protein interface. The relevance of these structures with respect to the measured changes in affinity between MauG and various forms of MADH is discussed. PubMed: 23832199DOI: 10.1107/S1744309113016539 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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