1YE9

Crystal structure of proteolytically truncated catalase HPII from E. coli

Summary for 1YE9

• Entry DOI: 10.2210/pdb1ye9/pdb
• Related: 1GGE
• Descriptor: catalase HPII, CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE, ... (4 entities in total)
• Functional Keywords: catalase hpii, proteolytic truncation, beta barrel core, oxidoreductase
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm (Probable): P21179 P21179
• Total number of polymer chains: 16
• Total formula weight: 450565.96

Authors

Loewen, P.C.,Chelikani, P.,Carpena, X.,Fita, I.,Perez-Luque, R.,Donald, L.J.,Switala, J.,Duckworth, H.W. (deposition date: 2004-12-28, release date: 2005-04-26, Last modification date: 2023-10-25)

Primary citation

Chelikani, P.,Carpena, X.,Perez-Luque, R.,Donald, L.J.,Duckworth, H.W.,Switala, J.,Fita, I.,Loewen, P.C.
Characterization of a Large Subunit Catalase Truncated by Proteolytic Cleavage(,)
Biochemistry, 44:5597-5605, 2005

PubMed Abstract: The large subunit catalase HPII from Escherichia coli can be truncated by proteolysis to a structure similar to small subunit catalases. Mass spectrometry analysis indicates that there is some heterogeneity in the precise cleavage sites, but approximately 74 N-terminal residues, 189 C-terminal residues, and a 9-11-residue internal fragment, including residues 298-308, are removed. Crystal structure refinement at 2.8 A reveals that the tertiary and quaternary structure of the native enzyme is retained with only very subtle changes despite the loss of 36% of the sequence. The truncated variant exhibits a 1.8 times faster turnover rate and enhanced sensitivity to high concentrations of H(2)O(2), consistent with easier access of the substrate to the active site. In addition, the truncated variant is more sensitive to inhibition, particularly by reagents such as aminotriazole and azide which are larger than substrate H(2)O(2). The main channel leading to the heme cavity is largely unaffected by the truncation, but the lateral channel is shortened and its entrance widened by removal of the C-terminal domain, providing an explanation for easier access to the active site. Opening of the entrance to the lateral channel also opens the putative NADPH binding site, but NADPH binding could not be demonstrated. Despite the lack of bound NADPH, the compound I species of both native and truncated HPII are reduced back to the resting state with compound II being evident in the absorbance spectrum only of the heme b-containing H392A variant.

PubMed: 15823018
DOI: 10.1021/bi047277m

Experimental method

X-RAY DIFFRACTION (2.8 Å)