Structure of Stenotrophomonas maltophilia FeoA complexed with zinc: A unique prokaryotic SH3 - Domain protein that possibly acts as a bacterial ferrous iron-transport activating factor

Yi Che Su, Ko Hsin Chin, Hui Chih Hung, Gwan Han Shen, Andrew H.J. Wang, Shan Ho Chou

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)

Abstract

Iron is vital to the majority of prokaryotes, with ferrous iron believed to be the preferred form for iron uptake owing to its much better solubility. The major route for bacterial ferrous iron uptake is found to be via an Feo (ferrous iron-transport) system comprising the three proteins FeoA, FeoB and FeoC. Although the structure and function of FeoB have received much attention recently, the roles played by FeoA and FeoC have been little investigated to date. Here, the tertiary structure of FeoA from Stenotrophomonas maltophilia (Sm), a vital opportunistic pathogen in immunodepressed hosts, is reported. The crystal structure of SmFeoA has been determined to a resolution of 1.7 Å using an Se single-wavelength anomalous dispersion (Se-SAD) approach. Although SmFeoA bears low sequence identity to eukaryotic proteins, its structure is found to adopt a eukaryotic SH3-domain-like fold. It also bears weak similarity to the C-terminal SH3 domain of bacterial DtxR (diphtheria toxin regulator), with some unique characteristics. Intriguingly, SmFeoA is found to adopt a unique dimer cross-linked by two zinc ions and six anions (chloride ions). Since FeoB has been found to contain a G-protein-like domain with low GTPase activity, FeoA may interact with FeoB through the SH3-G-protein domain interaction to act as a ferrous iron-transport activating factor.

Original languageEnglish
Pages (from-to)636-642
Number of pages7
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number6
DOIs
Publication statusPublished - 2010
Externally publishedYes

Keywords

  • FeoA
  • Ferrous iron transport
  • Prokaryotic SH3 domain
  • Stenotrophomonus maltophilia
  • Zinc binding

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

Fingerprint

Dive into the research topics of 'Structure of Stenotrophomonas maltophilia FeoA complexed with zinc: A unique prokaryotic SH3 - Domain protein that possibly acts as a bacterial ferrous iron-transport activating factor'. Together they form a unique fingerprint.

Cite this