Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1-Å resolution

Edwards, Ross A.; Baker, Heather M.; Whittaker, Mei M.; Whittaker, James W.; Jameson, Geoffrey B.; Baker, Edward N.

doi:10.1007/s007750050217

Cited by 139 publications

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“…Seven structures of MnSODs have been reported, three of which are tetrameric [human MnSOD (Borgstahl et al, 1992), Thermus thermophilus MnSOD (Ludwig et al, 1991) and Aspergillus fumigatus MnSOD (Fluckiger et al, 2002)], while the others are dimeric [Escherichia coli MnSOD (Edwards et al, 1998), Bacillus stearothermophilus MnSOD (Parker & Blake, 1988), Bacillus anthracis MnSOD (Boucher et al, 2005), Deinococcus radiodurans MnSOD (Dennis et al, 2006) and cyanobacterium MnSOD (Atzenhofer et al, 2002)]. All the structures share a common overall fold with the ironcontaining enzymes.…”

Section: Resultsmentioning

confidence: 99%

Purification, crystallization and X-ray structures of the two manganese superoxide dismutases fromCaenorhabditis elegans

et al. 2008

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PDB References: manganese superoxide dismutase 3dc6, r3dc6sf; 3dc5, r3dc5sf. Caenorhabditis elegans expresses two manganese superoxide dismutase enzymes (MnSOD-2 and MnSOD-3) that are targeted to the mitochondrion. MnSOD-2 is constitutively expressed, while synthesis of MnSOD-3 is inducible. The structures of these two mononuclear metalloenzymes have been determined to 1.8 and 1.7 Å resolution, respectively. Pink crystals formed in space group P4 1 2 1 2 for each, with unit-cell parameters a = b = 81.0, c = 137.4 Å for MnSOD-2 and a = b = 81.8, c = 136.0 Å for MnSOD-3. The final structure of MnSOD-3 was refined to R = 21.6% and R free = 26.2% at 293 K, and R = 18.9% and R free = 22.6% at 100 K, while that of MnSOD-2 was refined to R = 16.9% and R free = 20.1% at 100 K. The asymmetric unit cell is comprised of two subunits. The resulting structures are very similar to that of human MnSOD and form a tetramer corresponding to a dimer of dimers. The subunit interface between dimers is comprised of two four-helix bundles that stabilize the biologically significant homotetramer.

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Section: Resultsmentioning

confidence: 99%

Purification, crystallization and X-ray structures of the two manganese superoxide dismutases fromCaenorhabditis elegans

et al. 2008

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“…A very low pK ox will tend to decrease the E m whereas a low pK red will raise E m much less since K red is smaller than [H + ] [eq 2, where K ox and K red are the acid dissociation constants of the oxidized and reduced states, respectively, E AH is the reduction potential of the fully protonated species, E m is the potential observed at a given pH, and pK ) -log(K)]. 6 In addition, protonation 5 The different active site conformation observed in the Fe(Mn)-SOD crystal structure can most simply be ascribed to the fact that this structure was obtained at a pH well above the pK ascribed to OHbinding (1) whereas the structure of MnSOD was determined at a pH well below the pK ascribed to OH -binding (53 (31,43,49), and the titrations should properly be considered to be in quasi-equilibrium. Thus, the SODs' Ems may incorporate substantial uncertainty despite our best efforts.…”

Section: Discussionmentioning

confidence: 99%

Novel Insights into the Basis for Escherichia coli Superoxide Dismutase's Metal Ion Specificity from Mn-Substituted FeSOD and Its Very High E_m

2001

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Fe and Mn are both entrained to the same chemical reaction in apparently superimposable superoxide dismutase (SOD) proteins. However, neither Fe-substituted MnSOD nor Mn-substituted FeSOD is active. We have proposed that the two SOD proteins must apply very different redox tuning to their respective metal ions and that tuning appropriate for one metal ion results in a reduction potential (E m ) for the other metal ion that is either too low (Fe) or too high (Mn) [Vance and Miller (1998) J. Am. Chem. Soc. 120, 461-467]. We have demonstrated that this is true for Fe-substituted MnSOD from Escherichia coli and that this metal ion-protein combination retains the ability to reduce but not oxidize superoxide. We now demonstrate that the corollary is also true: Mn-substituted FeSOD [Mn(Fe)SOD] has a very high E m . Specifically, we have measured the E m of E. coli MnSOD to be 290 mV vs NHE. We have generated Mn(Fe)SOD and find that Mn is bound in an environment similar to that of the native (Mn)SOD protein. However, the E m is greater than 960 mV vs NHE and much higher than MnSOD's E m of 290 mV. We propose that the different tuning stems from different hydrogen bonding between the proteins and a molecule of solvent that is coordinated to the metal ion in both cases. Because a proton is taken up by SOD upon reduction, the protein can exert very strong control over the E m , by modulating the degree to which coordinated solvent is protonated, in both oxidation states. Thus, coordinated solvent molecules may have widespread significance as "adapters" by which proteins can control the reactivity of bound metal ions.

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“…The structure of SpMnSOD1 was determined using molecular replacement using the MnSOD structure from Bacillus subtilis (pdb: 2RCV). 23 The coli (pdb code 1D5N), 21 T. thermophilus (pdb code 3MDS), 22 B. subtilis (pdb code 2RCV), 23 D.…”

Section: Crystal Structure Of Mnsod1mentioning

confidence: 99%

“…21 All of the Mn ligands and gateway residues are conserved in the primary sequence, and can be superimposed with only very small perturbations in structure (see Figure 5B). However, there are some amino acid replacements near the active site, shown in Figure 6.…”

Section: Crystal Structure Of Mnsod1mentioning

confidence: 99%

Identification of Manganese Superoxide Dismutase from Sphingobacterium sp. T2 as a Novel Bacterial Enzyme for Lignin Oxidation

et al. 2015

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Copyright and reuse:The Warwick Research Archive Portal (WRAP) makes this work of researchers of the University of Warwick available open access under the following conditions. Copyright © and all moral rights to the version of the paper presented here belong to the individual author(s) and/or other copyright owners. To the extent reasonable and practicable the material made available in WRAP has been checked for eligibility before being made available.Copies of full items can be used for personal research or study, educational, or not-forprofit purposes without prior permission or charge. Provided that the authors, title and full bibliographic details are credited, a hyperlink and/or URL is given for the original metadata page and the content is not changed in any way. Publisher's statement:This document is the Accepted Manuscript version of a Published Work that appeared in final form in ACS Chemical Biology, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see: http://dx.doi.org/10.1021/acschembio.5b00298The version presented here may differ from the published version or, version of record, if you wish to cite this item you are advised to consult the publisher's version. Please see the 'permanent WRAP url' above for details on accessing the published version and note that access may require a subscription. centre ligated by three His, one Asp and a water/hydroxide in each active site. We propose that the lignin oxidation reactivity of these enzymes is due to the production of hydroxyl radical, a highly reactive oxidant. This is the first demonstration that MnSOD is a microbial lignin-oxidising enzyme.3

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Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1-Å resolution

Cited by 139 publications

References 0 publications

Purification, crystallization and X-ray structures of the two manganese superoxide dismutases fromCaenorhabditis elegans

Purification, crystallization and X-ray structures of the two manganese superoxide dismutases fromCaenorhabditis elegans

Novel Insights into the Basis for Escherichia coli Superoxide Dismutase's Metal Ion Specificity from Mn-Substituted FeSOD and Its Very High E_m

Identification of Manganese Superoxide Dismutase from Sphingobacterium sp. T2 as a Novel Bacterial Enzyme for Lignin Oxidation

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Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1-Å resolution

Cited by 139 publications

References 0 publications

Purification, crystallization and X-ray structures of the two manganese superoxide dismutases fromCaenorhabditis elegans

Purification, crystallization and X-ray structures of the two manganese superoxide dismutases fromCaenorhabditis elegans

Novel Insights into the Basis for Escherichia coli Superoxide Dismutase's Metal Ion Specificity from Mn-Substituted FeSOD and Its Very High Em

Identification of Manganese Superoxide Dismutase from Sphingobacterium sp. T2 as a Novel Bacterial Enzyme for Lignin Oxidation

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Novel Insights into the Basis for Escherichia coli Superoxide Dismutase's Metal Ion Specificity from Mn-Substituted FeSOD and Its Very High E_m