The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension(525 views) Esposito L, Seydel A, Aiello R, Sorrentino G, Cendron L, Zanotti G, Zagari
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, I-80134 Naples, Italy
Deparment of Chemistry, University of Padua, Institute of Biomolecular Chemistry, Padua, Italy
Venetian Institute of Molecular Medicine (VIMM), Padua, Italy
Department of Biological Sciences, CNISM, University of Naples Federico II, Naples, Italy
CEINGE, Advanced Biotechnologies, Scarl, Naples, Italy
References: Not available.
The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension
Superoxide dismutases (SODs) are key enzymes for fighting oxidative stress. Helicobacter pylori produces a single SOD (HpSOD) which contains iron. The structure of this antioxidant protein has been determined at 2.4 angstrom resolution. It is a dimer of two identical subunits with one iron ion per monomer. The protein shares 53% sequence identity with the corresponding enzyme from Escherichia coli. The model is compared with those of other dimeric Fe-containing SODs. HpSOD shows significant differences in relation to other SODs, the most important being an extended C-terminal tail. This structure provides a model for closely related sequences from species such as Campylobacter, where no structures are currently known. The structure of extended carboxyl termini is discussed in light of putative functions it may serve. (C) 2008 Elsevier B.V. All rights reserved.
The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension
Vitiello M, Finamore E, Falanga A, Raieta K, Cantisani M, Galdiero F, Pedone C, Galdiero M, Galdiero S * Fusion in Coq(578 views) Lecture Notes In Computer Science (ISSN: 0302-9743, 0302-974335404636319783540463634, 0302-974335402975459783540297543), 2001; 2178LNCS: 583-596. Impact Factor:0.415 ViewExport to BibTeXExport to EndNote