2b2r
From Proteopedia
Crystal structure of an oxoferryl species of catalase-peroxidase KATG at pH5.6
Overview
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.
About this Structure
2B2R is a Single protein structure of sequence from Burkholderia pseudomallei. Full crystallographic information is available from OCA.
Reference
A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidases., Carpena X, Wiseman B, Deemagarn T, Singh R, Switala J, Ivancich A, Fita I, Loewen PC, EMBO Rep. 2005 Dec;6(12):1156-62. PMID:16211084 Page seeded by OCA on Sat May 3 19:46:35 2008
