4BR6

Crystal structure of Chaetomium thermophilum MnSOD

Summary for 4BR6

• Entry DOI: 10.2210/pdb4br6/pdb
• Descriptor: SUPEROXIDE DISMUTASE, MANGANESE (III) ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: oxidoreductase, dismutation, antioxidants, thermostability, metal binding
• Biological source: CHAETOMIUM THERMOPHILUM
• Total number of polymer chains: 4
• Total formula weight: 87895.51

Authors

Haikarainen, T.,Frioux, C.,Zhnag, L.-Q.,Li, D.-C.,Papageorgiou, A.C. (deposition date: 2013-06-04, release date: 2013-12-18, Last modification date: 2023-12-20)

Primary citation

Haikarainen, T.,Frioux, C.,Zhnag, L.,Li, D.,Papageorgiou, A.C.
Crystal Structure and Biochemical Characterization of a Manganese Superoxide Dismutase from Chaetomium Thermophilum.
Biochim.Biophys.Acta, 1844:422-, 2014

PubMed Abstract: A manganese superoxide dismutase from the thermophilic fungus Chaetomium thermophilum (CtMnSOD) was expressed in Pichia pastoris and purified to homogeneity. Its optimal temperature was 60°C with approximately 75% of its activity retained after incubation at 70°C for 60min. Recombinant yeast cells carrying C. thermophilum mnsod gene exhibited higher stress resistance to salt and oxidative stress-inducing agents than control yeast cells. In an effort to provide structural insights, CtMnSOD was crystallized and its structure was determined at 2.0Å resolution. The overall architecture of CtMnSOD was found similar to other MnSODs with highest structural similarities obtained against a MnSOD from the thermotolerant fungus Aspergillus fumigatus. In order to explain its thermostability, structural and sequence analysis of CtMnSOD with other MnSODs was carried out. An increased number of charged residues and an increase in the number of intersubunit salt bridges and the Thr:Ser ratio were identified as potential reasons for the thermostability of CtMnSOD.

PubMed: 24316252
DOI: 10.1016/J.BBAPAP.2013.11.014

Experimental method

X-RAY DIFFRACTION (2 Å)