1MQF

Compound I from Proteus mirabilis catalase

Replaces:  2CAF

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: 2011-07-13)

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

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: 14646074
DOI: 10.1107/S0907444903019620

Experimental method

X-RAY DIFFRACTION (2.5 Å)