Literature DB >> 6346322

Iron superoxide dismutase from Escherichia coli at 3.1-A resolution: a structure unlike that of copper/zinc protein at both monomer and dimer levels.

W C Stallings, T B Powers, K A Pattridge, J A Fee, M L Ludwig.   

Abstract

The structure of iron superoxide dismutase (EC 1.15.1.1) from Escherichia coli has been determined at 3.1-A resolution. The dimeric molecule is constructed from identical subunits, which are two-domain polypeptides. The NH2-terminal domain is composed of two antiparallel crossing helices and the COOH-terminal domain is a three-layered structure characterized by mixed alpha/beta secondary structural features. The active center iron atoms, separated by 18 A and located near the monomer-monomer interface, are coordinated by two amino acid residues from each domain. Azide binding has been investigated by using difference Fourier techniques. Consistent with the notion of the independent evolution of the copper/zinc dismutase gene, the iron dismutase structure resembles the copper/zinc protein at neither the monomer nor the dimer level.

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Year:  1983        PMID： 6346322      PMCID： PMC394163          DOI： 10.1073/pnas.80.13.3884

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


  32 in total

1.  Quaternary and tertiary structure of haemerythrin.

Authors:  K B Ward; W A Hendrickson; G L Klippenstein
Journal:  Nature       Date:  1975-10-30       Impact factor: 49.962

2.  Tertiary structure of myohemerythrin at low resolution.

Authors:  W A Hendrickson; G L Klippenstein; K B Ward
Journal:  Proc Natl Acad Sci U S A       Date:  1975-06       Impact factor: 11.205

3.  Superoxide dismutase in some obligately anaerobic bacteria.

Authors:  J Hewitt; J G Morris
Journal:  FEBS Lett       Date:  1975-02-15       Impact factor: 4.124

4.  Subcellular localization of superoxide dismutase in rat liver.

Authors:  C Peeters-Joris; A M Vandevoorde; P Baudhuin
Journal:  Biochem J       Date:  1975-07       Impact factor: 3.857

5.  Purification, crystallization and properties of iron-containing superoxide dismutase from Pseudomonas ovalis.

Authors:  F Yamakura
Journal:  Biochim Biophys Acta       Date:  1976-02-13

6.  Sequence homologies among bacterial and mitochondrial superoxide dismutases.

Authors:  H M Steinman; R L Hill
Journal:  Proc Natl Acad Sci U S A       Date:  1973-12       Impact factor: 11.205

7.  Comparison of super-secondary structures in proteins.

Authors:  S T Rao; M G Rossmann
Journal:  J Mol Biol       Date:  1973-05-15       Impact factor: 5.469

8.  Superoxide dismutase in the anaerobic flagellates, Tritrichomonas foetus and Monocercomonas sp.

Authors:  D G Lindmark; M Müller
Journal:  J Biol Chem       Date:  1974-07-25       Impact factor: 5.157

9.  Mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysis.

Authors:  E M Fielden; P B Roberts; R C Bray; D J Lowe; G N Mautner; G Rotilio; L Calabrese
Journal:  Biochem J       Date:  1974-04       Impact factor: 3.857

10.  Crystal structure of bovine Cu,Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands.

Authors:  J Richardson; K A Thomas; B H Rubin; D C Richardson
Journal:  Proc Natl Acad Sci U S A       Date:  1975-04       Impact factor: 11.205
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  15 in total

1.  Identification of negative cis-acting elements in response to copper in the chloroplastic iron superoxide dismutase gene of the moss Barbula unguiculata.

Authors:  Miwa Nagae; Masaru Nakata; Yohsuke Takahashi
Journal:  Plant Physiol       Date:  2008-02-07       Impact factor: 8.340

2.  Cloning of the sodA gene from Corynebacterium melassecola and role of superoxide dismutase in cellular viability.

Authors:  M Merkamm; A Guyonvarch
Journal:  J Bacteriol       Date:  2001-02       Impact factor: 3.490

3.  Non-homologous isofunctional enzymes: a systematic analysis of alternative solutions in enzyme evolution.

Authors:  Marina V Omelchenko; Michael Y Galperin; Yuri I Wolf; Eugene V Koonin
Journal:  Biol Direct       Date:  2010-04-30       Impact factor: 4.540

Review 4.  Superoxide dismutases and superoxide reductases.

Authors:  Yuewei Sheng; Isabel A Abreu; Diane E Cabelli; Michael J Maroney; Anne-Frances Miller; Miguel Teixeira; Joan Selverstone Valentine
Journal:  Chem Rev       Date:  2014-04-01       Impact factor: 60.622

Review 5.  Protein design: toward functional metalloenzymes.

Authors:  Fangting Yu; Virginia M Cangelosi; Melissa L Zastrow; Matteo Tegoni; Jefferson S Plegaria; Alison G Tebo; Catherine S Mocny; Leela Ruckthong; Hira Qayyum; Vincent L Pecoraro
Journal:  Chem Rev       Date:  2014-03-24       Impact factor: 60.622

6.  The crystal structure of an eukaryotic iron superoxide dismutase suggests intersubunit cooperation during catalysis.

Authors:  Inés G Muñoz; Jose F Moran; Manuel Becana; Guillermo Montoya
Journal:  Protein Sci       Date:  2005-02       Impact factor: 6.725

7.  Structure of iron superoxide dismutase from Pseudomonas ovalis at 2.9-A resolution.

Authors:  D Ringe; G A Petsko; F Yamakura; K Suzuki; D Ohmori
Journal:  Proc Natl Acad Sci U S A       Date:  1983-07       Impact factor: 11.205

8.  Construction of a catalytically active iron superoxide dismutase by rational protein design.

Authors:  A L Pinto; H W Hellinga; J P Caradonna
Journal:  Proc Natl Acad Sci U S A       Date:  1997-05-27       Impact factor: 11.205

9.  Cloning and characterization of an Anacystis nidulans R2 superoxide dismutase gene.

Authors:  D E Laudenbach; C G Trick; N A Straus
Journal:  Mol Gen Genet       Date:  1989-04

10.  Analysis of Soluble protein complexes in Shigella flexneri reveals the influence of temperature on the amount of lipopolysaccharide.

Authors:  Chang Niu; Na Shang; Xiang Liao; Erling Feng; Xiankai Liu; Dongshu Wang; Jie Wang; Peitang Huang; Yuejin Hua; Li Zhu; Hengliang Wang
Journal:  Mol Cell Proteomics       Date:  2013-02-02       Impact factor: 5.911
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