1si8
Crystal structure of E. faecalis catalase
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | katA (Enterococcus faecalis) | ||||||
| Activity: | Catalase, with EC number 1.11.1.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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 A. The three-dimensional structure was determined by molecular replacement using a subunit of the Proteus mirabilis catalase structure. It was refined against 2.3 A 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.
About this StructureAbout this Structure
1SI8 is a Single protein structure of sequence from Enterococcus faecalis. Full crystallographic information is available from OCA.
ReferenceReference
The three-dimensional structure of catalase from Enterococcus faecalis., Hakansson KO, Brugna M, Tasse L, Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1374-80. Epub 2004, Jul 21. PMID:15272159
Page seeded by OCA on Sun Mar 30 23:42:28 2008