Structural Studies on Flavodiiron Proteins

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

24 Citations (Scopus)

Abstract

Crystallographic studies on flavodiiron proteins (FDPs) have revealed that the common sequence core (≈400 residues) that defines this protein family comprises two structural domains. The N-terminal domain (of approximately 250 residues) displays a metallo-β-lactamase-like-fold, being indeed structurally homologous to β-lactamases and glyoxalases, despite the poor sequence similarity. Whereas β-lactamases have mono- or dizinc sites and glyoxalases a mixed iron-zinc site, the lactamase domain of FDPs harbors a nonheme diiron center with carboxylate and histidine residues as ligands, assigned as the active site of NO and/or O2 reduction. The C-terminal domain of FDPs is characterized by a flavodoxin-like fold, homologous to short-chain flavodoxins, and harbors a flavin mononucleotide moiety, stabilized by van der Waals interactions and a number of hydrogen bonds. Structures of FDPs obtained in different conditions and oxidation states display some heterogeneities, mostly at the diiron site, but still fail to provide unequivocal evidence for some pending questions regarding the substrate activation mechanism of FDPs, namely the preference for either substrate (NO or oxygen) observed in different members of this protein family. More structural studies are therefore required to achieve a deeper understanding on these matters.

Original languageEnglish
Title of host publicationGlobins and Other Nitric Oxide-Reactive Proteins, Part B
PublisherAcademic Press Inc.
Pages3-19
Number of pages17
ISBN (Print)9780123742780
DOIs
Publication statusPublished - 1 Jan 2008

Publication series

NameMethods in Enzymology
Volume437
ISSN (Print)0076-6879

Keywords

  • electron transferring flavoprotein
  • flavoproteiniron
  • carboxylic acid
  • glyoxalase
  • histidine
  • metallo beta lactamase
  • nitric oxide
  • oxygen
  • beta lactamase
  • flavodoxin
  • flavine mononucleotide

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