Structure of the manganese superoxide dismutase from Deinococcus radiodurans in two crystal forms
Open accessAbstract
The structure of the manganese superoxide dismutase (Mn-SOD; DR1279) from Deinococcus radiodurans has been determined in two different crystal forms. Both crystal forms are monoclinic with space group P2(1). Form I has unit-cell parameters a = 44.28, b = 83.21, c = 59.52 angstroms, beta = 110.18 degrees and contains a homodimer in the asymmetric unit, with structure refinement (R = 16.8%, R(free) = 23.6%) carried out using data to d(min) = 2.2 angstroms. Form II has unit-cell parameters a = 43.57, b = 87.10, c = 116.42 angstroms, beta = 92.1 degrees and an asymmetric unit containing two Mn-SOD homodimers; structure refinement was effected to a resolution of 2.0 angstroms (R = 17.2%, R(free) = 22.3%). The resulting structures are compared with that of Mn-SOD from Escherichia coli, with which they are shown to be essentially isostructural.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The active sites and structures of three MnSODs (human, Escherichia coli, and Deinococcus radiodurans) have been studied in detail.
“The active sites and structures of three MnSODs (human, Escherichia coli, and Deinococcus radiodurans) have been studied in detail [80,81,82].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [81]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617 · see citing works
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147 · see citing works
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,720 · see citing works
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,650 · see citing works
AMoRe: an automated package for molecular replacement
Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,941 · see citing works
Use of TLS parameters to model anisotropic displacements in macromolecular refinement
Winn, M., Isupov, M. N., & Murshudov, G. N. (2001) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444900014736 · Cited by 1,701 · see citing works
Gouet, P. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg556 · Cited by 1,505 · see citing works
Biological effects of the superoxide radical
Fridovich, I. (1986) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(86)90526-6 · Cited by 1,422 · see citing works
Makarova, K. S., Aravind, L., Wolf, Y. I., Tatusov, R. L., Minton, K. W., Koonin, E. V., & Daly, M. J. (2001) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.65.1.44-79.2001 · Cited by 733 · see citing works
Mattimore, V, & Battista, J. R. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.3.633-637.1996 · Cited by 687 · see citing works
AGAINST ALL ODDS: The Survival Strategies of Deinococcus radiodurans
Battista, J. R. (1997) · Annual Review of Microbiology · doi:10.1146/annurev.micro.51.1.203 · Cited by 571 · see citing works
DNA repair in the extremely radioresistant bacterium Deinococcus radiodurans
Minton, K. W. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb00397.x · Cited by 292 · see citing works
Ringlike Structure of the Deinococcus radiodurans Genome: A Key to Radioresistance?
Levin‐Zaidman, S., Englander, J., Shimoni, E., Sharma, A. K., Minton, K. W., & Minsky, A. (2003) · Science · doi:10.1126/science.1077865 · Cited by 245 · see citing works
Parker, M. W., & Blake, C. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)81160-8 · Cited by 243 · see citing works
Markillie, L. M., Varnum, S. M., Hradecky, P., & Wong, K. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.2.666-669.1999 · Cited by 141 · see citing works
Superoxide dismutase and the oxygen enhancement of radiation lethality
Misra, H. P., & Fridovich, I. (1976) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(76)90201-0 · Cited by 139 · see citing works
Functional differences between manganese and iron superoxide dismutases in Escherichia coli K-12.
Hopkin, K., Papazian, M., & Steinman, H. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35758-2 · Cited by 102 · see citing works
Borgstahl, G. E. O., Pokross, M. E., Chehab, R., Sekher, A., & Snell, E. H. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3506 · Cited by 73 · see citing works
Chou, F. I., & Tan, S. T. (1990) · Journal of Bacteriology · doi:10.1128/jb.172.4.2029-2035.1990 · Cited by 71 · see citing works
The manganese superoxide dismutase of Escherichia coli K-12 associates with DNA.
Steinman, H. M., Weinstein, L., & Brenowitz, M. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61951-4 · Cited by 51 · see citing works
Edwards, R. A., Whittaker, M. M., Whittaker, J. W., Baker, E. N., & Jameson, G. B. (2001) · Biochemistry · doi:10.1021/bi002403h · Cited by 38 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- Lipton, M. S. et al. (2002). Proc. Natl Acad. Sci. USA, 99, 11049-11054.
Cited by
Sorted by citations
Superoxide dismutases—A review of the metal-associated mechanistic variations
Abreu, I. A., & Cabelli, D. E. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.11.005 · Cited by 563 · see citing works
Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342 · see citing works
- Authors
- Dennis, R. J., Micossi, E., McCarthy, J., Moe, E., Gordon, E. J., Kozielski-Stuhrmann, S., Leonard, G. A., & McSweeney, S.
- Affiliations
- European Synchrotron Radiation Facility (FR)
- UiT The Arctic University of Norway (NO)
- Venue
- Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Published
- 2006-03-25
- Volume
- 62
- Issue
- 4
- Pages
- 325-329
- ISSN
- 1744-3091 (ISSN-L)
- PMC
- PMC2222570
- OpenAlex
- W2073218835
- Cited by
- 30
- References
- 21
- Citations by year
- 2026: 1 · 2023: 2 · 2022: 2 · 2021: 1 · 2020: 1 · 2019: 4 · 2018: 3 · 2017: 1 · 2015: 2 · 2014: 1 · 2013: 1 · 2012: 1
- FWCI
- 1.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Acta Crystallographica Section F Structural Biology and Crystallization Communications (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Chemistry › Inorganic Chemistry › Crystal structures of chemical compounds
- Keywords
- manganese superoxide dismutase, Deinococcus radiodurans, crystal structure, homodimer, isostructural comparison, radioresistance (biology), metalloenzymes
- MeSH terms
- Escherichia coli, Models, Molecular, Protein Conformation, Superoxide Dismutase, Crystallography, X-Ray, Deinococcus
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
