Summary for 1MQF
Entry DOI | 10.2210/pdb1mqf/pdb |
Related | 1E93 1M85 2CAG 2CAH |
Descriptor | Catalase, SULFATE ION, OXYGEN ATOM, ... (6 entities in total) |
Functional Keywords | alpha + beta, oxidoreductase |
Biological source | Proteus mirabilis |
Cellular location | Cytoplasm: P42321 |
Total number of polymer chains | 1 |
Total formula weight | 57123.37 |
Authors | Andreoletti, P.,Pernoud, A.,Sainz, G.,Gouet, P.,Jouve, H.M. (deposition date: 2002-09-16, release date: 2002-10-02, Last modification date: 2024-11-20) |
Primary citation | Andreoletti, P.,Pernoud, A.,Sainz, G.,Gouet, P.,Jouve, H.M. Structural studies of Proteus mirabilis catalase in its ground state, oxidized state and in complex with formic acid. Acta Crystallogr.,Sect.D, 59:2163-2168, 2003 Cited by PubMed Abstract: The structure of Proteus mirabilis catalase in complex with an inhibitor, formic acid, has been solved at 2.3 A resolution. Formic acid is a key ligand of catalase because of its ability to react with the ferric enzyme, giving a high-spin iron complex. Alternatively, it can react with two transient oxidized intermediates of the enzymatic mechanism, compounds I and II. In this work, the structures of native P. mirabilis catalase (PMC) and compound I have also been determined at high resolution (2.0 and 2.5 A, respectively) from frozen crystals. Comparisons between these three PMC structures show that a water molecule present at a distance of 3.5 A from the haem iron in the resting state is absent in the formic acid complex, but reappears in compound I. In addition, movements of solvent molecules are observed during formation of compound I in a cavity located away from the active site, in which a glycerol molecule is replaced by a sulfate. These results give structural insights into the movement of solvent molecules, which may be important in the enzymatic reaction. PubMed: 14646074DOI: 10.1107/S0907444903019620 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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