5SX0: Crystal Structure Of An Oxoferryl Species Of Catalase-peroxidase Katg At Ph7.5

Citation:
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.
PDB ID: 5SX0Download
MMDB ID: 142361
PDB Deposition Date: 2016/8/9
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 5SX0: dimeric; determined by author and by software (PISA)
Molecular Components in 5SX0
Label Count Molecule
Proteins (2 molecules)
1
Catalase-peroxidase
Molecule annotation
1
Catalase-peroxidase
Molecule annotation
Chemicals (14 molecules)
1
2
2
2
3
3
4
2
5
3
6
2
* Click molecule labels to explore molecular sequence information.

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