The three-dimensional structure of catalase from Enterococcus faecalis

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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.

Detaljer

Författare
  • KO Hakansson
  • Myriam Brugna
  • L Tasse
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Strukturbiologi
Originalspråkengelska
Sidor (från-till)1374-1380
TidskriftActa Crystallographica. Section D: Biological Crystallography
Volym60
StatusPublished - 2004
PublikationskategoriForskning
Peer review utfördJa