Crystal structure of the cyanide-inhibited Xenopus laevis Cu,Zn superoxide dismutase at 98 K

Kristina Djinovic Carugo, Andrea Battistoni, Maria Teresa Carrì, Fabio Polticelli, Alessandro Desideri, Giuseppe Rotilio, Alessandro Coda, Martino Bolognesi

Research output: Contribution to journalArticle

Abstract

The crystal structure of cyanide-inhibited X. laevis Cu,Zn superoxide dismutase has been studied and refined based on diffraction data collected at 98 K. The final R-factor for the 27,299 reflections in the 10.0-1.7 Å resolution range is 0.170. The cyanide anion, which is a competitive inhibitor expected to mimic the superoxide binding mode, binds directly to the active site copper atom, replacing the coordinated water molecule. Moreover, the anion establishes a strong electrostatic interaction with the guanidinium group of the conserved active site residue Arg141. The coordination sphere of Cu2+ is partly altered with respect to the uninhibited enzyme: a displacement of 0.41 Å in subunit A, and 0.27 Å in subunit B of the dimeric enzyme is observed for the Cu2+ ions. Only two ligands in the Cu2+ coordination sphere (His46 and His118) are significantly affected by cyanide binding, whereas virtually no rearrangement of the Zn2+ ligands is reported.

Original languageEnglish
Pages (from-to)93-98
Number of pages6
JournalFEBS Letters
Volume349
Issue number1
DOIs
Publication statusPublished - Jul 25 1994

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Keywords

  • Crystal structure
  • Cyanide inhibition
  • Superoxide dismutase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Carugo, K. D., Battistoni, A., Carrì, M. T., Polticelli, F., Desideri, A., Rotilio, G., Coda, A., & Bolognesi, M. (1994). Crystal structure of the cyanide-inhibited Xenopus laevis Cu,Zn superoxide dismutase at 98 K. FEBS Letters, 349(1), 93-98. https://doi.org/10.1016/0014-5793(94)00651-2