The three-dimensional structure of catalase from Enterococcus faecalis
(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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https://lup.lub.lu.se/record/272613
- author
- Hakansson, KO ; Brugna, Myriam LU and Tasse, L
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Acta Crystallographica. Section D: Biological Crystallography
- volume
- 60
- pages
- 1374 - 1380
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000222791700004
- scopus:16644362979
- ISSN
- 1399-0047
- DOI
- 10.1107/S0907444904012004
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Department of Cell and Organism Biology (Closed 2011.) (011002100)
- id
- 27f95980-e817-4fed-ae1e-776909556232 (old id 272613)
- date added to LUP
- 2016-04-01 16:51:45
- date last changed
- 2022-01-28 22:39:30
@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 = {{John Wiley & Sons Inc.}}, 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}}, doi = {{10.1107/S0907444904012004}}, volume = {{60}}, year = {{2004}}, }