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The three-dimensional structure of catalase from Enterococcus faecalis

Hakansson, KO; Brugna, Myriam LU and Tasse, L (2004) In Acta Crystallographica. Section D: Biological Crystallography 60. p.1374-1380
Abstract
Enterococcus faecalis haem catalase was crystallized using lithium sulfate at neutral pH. The crystals belong to space group R3, with unit-cell parameters a = b = 236.9, c = 198.1 Angstrom. The three-dimensional structure was determined by molecular replacement using a subunit of the Proteus mirabilis catalase structure. It was refined against 2.3 Angstrom synchrotron data to a free R factor of 21.8%. Like other catalases, the E. faecalis catalase is a homotetramer with a fold and structure similar to those of its structurally closest relative P. mirabilis. The solvent structure in the active site is identical in the four subunits but differs from that found in other catalases. The structural consequences of the Ramachandran outlier Ser196... (More)
Enterococcus faecalis haem catalase was crystallized using lithium sulfate at neutral pH. The crystals belong to space group R3, with unit-cell parameters a = b = 236.9, c = 198.1 Angstrom. The three-dimensional structure was determined by molecular replacement using a subunit of the Proteus mirabilis catalase structure. It was refined against 2.3 Angstrom synchrotron data to a free R factor of 21.8%. Like other catalases, the E. faecalis catalase is a homotetramer with a fold and structure similar to those of its structurally closest relative P. mirabilis. The solvent structure in the active site is identical in the four subunits but differs from that found in other catalases. The structural consequences of the Ramachandran outlier Ser196 are discussed. (Less)
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type
Contribution to journal
publication status
published
subject
in
Acta Crystallographica. Section D: Biological Crystallography
volume
60
pages
1374 - 1380
publisher
International Union of Crystallography
external identifiers
  • wos:000222791700004
  • scopus:16644362979
ISSN
1399-0047
DOI
10.1107/S0907444904012004
language
English
LU publication?
yes
id
27f95980-e817-4fed-ae1e-776909556232 (old id 272613)
date added to LUP
2007-10-29 10:42:04
date last changed
2017-01-01 07:17:17
@article{27f95980-e817-4fed-ae1e-776909556232,
  abstract     = {Enterococcus faecalis haem catalase was crystallized using lithium sulfate at neutral pH. The crystals belong to space group R3, with unit-cell parameters a = b = 236.9, c = 198.1 Angstrom. The three-dimensional structure was determined by molecular replacement using a subunit of the Proteus mirabilis catalase structure. It was refined against 2.3 Angstrom synchrotron data to a free R factor of 21.8%. Like other catalases, the E. faecalis catalase is a homotetramer with a fold and structure similar to those of its structurally closest relative P. mirabilis. The solvent structure in the active site is identical in the four subunits but differs from that found in other catalases. The structural consequences of the Ramachandran outlier Ser196 are discussed.},
  author       = {Hakansson, KO and Brugna, Myriam and Tasse, L},
  issn         = {1399-0047},
  language     = {eng},
  pages        = {1374--1380},
  publisher    = {International Union of Crystallography},
  series       = {Acta Crystallographica. Section D: Biological Crystallography},
  title        = {The three-dimensional structure of catalase from Enterococcus faecalis},
  url          = {http://dx.doi.org/10.1107/S0907444904012004},
  volume       = {60},
  year         = {2004},
}