5Y17

CATPO mutant - E316F

Summary for 5Y17

• Entry DOI: 10.2210/pdb5y17/pdb
• Descriptor: Catalase, CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: catalase, phenol oxidase, lateral channel, mutant, oxidoreductase
• Biological source: Mycothermus thermophilus
• Total number of polymer chains: 4
• Total formula weight: 302027.07

Authors

Karakus Yuzugullu, Y.,Goc, G.,Balci, S.,Pearson, A.R.,Yorke, B. (deposition date: 2017-07-19, release date: 2018-07-25, Last modification date: 2023-11-22)

Primary citation

Yuzugullu Karakus, Y.,Goc, G.,Balci, S.,Yorke, B.A.,Trinh, C.H.,McPherson, M.J.,Pearson, A.R.
Identification of the site of oxidase substrate binding in Scytalidium thermophilum catalase.
Acta Crystallogr D Struct Biol, 74:979-985, 2018

PubMed Abstract: The catalase from Scytalidium thermophilum is a homotetramer containing a heme d in each active site. Although the enzyme has a classical monofunctional catalase fold, it also possesses oxidase activity towards a number of small organics, including catechol and phenol. In order to further investigate this, the crystal structure of the complex of the catalase with the classical catalase inhibitor 3-amino-1,2,4-triazole (3TR) was determined at 1.95 Å resolution. Surprisingly, no binding to the heme site was observed; instead, 3TR occupies a binding site corresponding to the NADPH-binding pocket in mammalian catalases at the entrance to a lateral channel leading to the heme. Kinetic analysis of site-directed mutants supports the assignment of this pocket as the binding site for oxidase substrates.

PubMed: 30289408
DOI: 10.1107/S2059798318010628

Experimental method

X-RAY DIFFRACTION (2.3 Å)