4O65
Crystal structure of the cupredoxin domain of amoB from Nitrosocaldus yellowstonii
Summary for 4O65
| Entry DOI | 10.2210/pdb4o65/pdb |
| Descriptor | Putative archaeal ammonia monooxygenase subunit B, COPPER (II) ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | cupredoxin, ammonia monooxygenase, amo, ammonia oxidation, ammonia, membrane, oxidoreductase |
| Biological source | Candidatus Nitrosocaldus yellowstonii |
| Total number of polymer chains | 1 |
| Total formula weight | 18412.09 |
| Authors | Lawton, T.J.,Ham, J.,Sun, T.,Rosenzweig, A.C. (deposition date: 2013-12-20, release date: 2014-04-02, Last modification date: 2024-10-16) |
| Primary citation | Lawton, T.J.,Ham, J.,Sun, T.,Rosenzweig, A.C. Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily. Proteins, 82:2263-2267, 2014 Cited by PubMed Abstract: The ammonia monooxygenase (AMO)/particulate methane monooxygenase (pMMO) superfamily is a diverse group of membrane-bound enzymes of which only pMMO has been characterized on the molecular level. The pMMO active site is believed to reside in the soluble N-terminal region of the pmoB subunit. To understand the degree of structural conservation within this superfamily, the crystal structure of the corresponding domain of an archaeal amoB subunit from Nitrosocaldus yellowstonii has been determined to 1.8 Å resolution. The structure reveals a remarkable conservation of overall fold and copper binding site location as well as several notable differences that may have implications for function and stability. PubMed: 24523098DOI: 10.1002/prot.24535 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.796 Å) |
Structure validation
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