5KSK
Crystal structure of the catalase-peroxidase from B. pseudomallei treated with acetate
Summary for 5KSK
| Entry DOI | 10.2210/pdb5ksk/pdb |
| Related | 5KQ0 5KQ2 5KQ3 5KQ6 5KQ7 5KQH 5KQI 5KQK 5KQN 5KQQ 5KSF 5KSG 5KSN 5KT8 5KT9 |
| Descriptor | Catalase-peroxidase, PROTOPORPHYRIN IX CONTAINING FE, SODIUM ION, ... (7 entities in total) |
| Functional Keywords | catalase, peroxidase, acetate, heme, oxidoreductase |
| Biological source | Burkholderia pseudomallei (strain 1710b) |
| Total number of polymer chains | 2 |
| Total formula weight | 161142.70 |
| Authors | Loewen, P.C. (deposition date: 2016-07-08, release date: 2017-04-26, Last modification date: 2023-11-15) |
| Primary citation | Machuqueiro, M.,Victor, B.,Switala, J.,Villanueva, J.,Rovira, C.,Fita, I.,Loewen, P.C. The Catalase Activity of Catalase-Peroxidases Is Modulated by Changes in the pKa of the Distal Histidine. Biochemistry, 56:2271-2281, 2017 Cited by PubMed Abstract: The unusual Met-Tyr-Trp adduct composed of cross-linked side chains along with an associated mobile Arg is essential for catalase activity in catalase-peroxidases. In addition, acidic residues in the entrance channel, in particular an Asp and a Glu ∼7 and ∼15 Å, respectively, from the heme, significantly enhance catalase activity. The mechanism by which these channel carboxylates influence catalase activity is the focus of this work. Seventeen new variants with fewer and additional acidic residues have been constructed and characterized structurally and for enzymatic activity, revealing that their effect on activity is roughly inversely proportional to their distance from the heme and adduct, suggesting that the electrostatic potential of the heme cavity may be affected. A discrete group of protonable residues are contained within a 15 Å sphere surrounding the heme iron, and a computational analysis reveals that the pK of the distal His, alone, is modulated within the pH range of catalase activity by the remote acidic residues in a pattern consistent with its protonated form having a key role in the catalase reaction cycle. The electrostatic potential also impacts the catalatic reaction through its influence on the charged status of the Met-Tyr-Trp adduct. PubMed: 28409923DOI: 10.1021/acs.biochem.6b01276 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.69 Å) |
Structure validation
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