2XQ1

Crystal structure of peroxisomal catalase from the yeast Hansenula polymorpha

Summary for 2XQ1

• Entry DOI: 10.2210/pdb2xq1/pdb
• Descriptor: PEROXISOMAL CATALASE, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: oxidoreductase, hydrogen peroxide detoxification, pts1
• Biological source: PICHIA ANGUSTA (HANSENULA POLYMORPHA)
• Cellular location: Peroxisome: P30263
• Total number of polymer chains: 16
• Total formula weight: 937803.99

Authors

Penya-Soler, E.,Vega, M.C.,Wilmanns, M.,Williams, C.P. (deposition date: 2010-08-31, release date: 2011-06-22, Last modification date: 2023-12-20)

Primary citation

Penya-Soler, E.,Vega, M.C.,Wilmanns, M.,Williams, C.P.
Structural Features of Peroxisomal Catalase from the Yeast Hansenula Polymorpha
Acta Crystallogr.,Sect.D, 67:690-, 2011

PubMed Abstract: The reactive oxygen species hydrogen peroxide is a byproduct of the β-oxidation process that occurs in peroxisomes. Since reactive oxygen species can cause serious damage to biomolecules, a number of scavengers control their intracellular levels. One such scavenger that is present in the peroxisome is the oxidoreductase catalase. In this study, the crystal structure of heterologously expressed peroxisomal catalase from the thermotolerant yeast Hansenula polymorpha has been determined at 2.9 Å resolution. H. polymorpha catalase is a typical peroxisomal catalase; it is tetrameric and is highly similar to catalases from other organisms. However, its hydrogen peroxide-degrading activity is higher than those of a number of other catalases for which structural data are available. Structural superimpositions indicate that the nature of the major channel, the path for hydrogen peroxide to the active site, varies from those seen in other catalase structures, an observation that may account for the high activity of H. polymorpha catalase.

PubMed: 21795810
DOI: 10.1107/S0907444911022463

Experimental method

X-RAY DIFFRACTION (2.9 Å)