5SW6

Crystal structure of an oxoferryl species of catalase-peroxidase KatG at pH5.6

Replaces:  2B2R

Summary for 5SW6

• Entry DOI: 10.2210/pdb5sw6/pdb
• Related: 5L02 5L05 5SW4 5SW5 5SX0 5SX1 5SX2 5SX3 5SX6 5SX7 5SXQ 5SXR 5SXS 5SXT 5SXX 5SYH 5SYI 5SYJ 5SYK 5SYL 5SYU 5SYV 5SYW 5SYX 5SYY
• Descriptor: Catalase-peroxidase, PROTOPORPHYRIN IX CONTAINING FE, SODIUM ION, ... (8 entities in total)
• Functional Keywords: catalase-peroxidase, katg, compound i, oxoferryl species, oxidoreductase
• Biological source: Burkholderia pseudomallei (strain 1710b)
• Total number of polymer chains: 2
• Total formula weight: 161025.38

Authors

Loewen, P.C. (deposition date: 2016-08-08, release date: 2016-08-24, Last modification date: 2024-10-09)

Primary citation

Carpena, X.,Wiseman, B.,Deemagarn, T.,Singh, R.,Switala, J.,Ivancich, A.,Fita, I.,Loewen, P.C.
A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidases.
EMBO Rep., 6:1156-1162, 2005

PubMed Abstract: The catalase reaction of catalase-peroxidases involves catalase-specific features built into a peroxidase core. An arginine, 20 A from the active-site heme, acts as a molecular switch moving between two conformations, one that activates heme oxidation and one that activates oxoferryl heme reduction by H(2)O(2), facilitating the catalatic pathway in a peroxidase. The influence of the arginine is imparted to the heme through its association with or dissociation from a tyrosinate that modulates reactivity through a Met-Tyr-Trp crosslinked adduct and a pi electron interaction of the heme with the adduct Trp.

PubMed: 16211084

Experimental method

X-RAY DIFFRACTION (1.9 Å)