NDLI: 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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Su, Yi Che Chin, Ko Hsin Hung, Hui Chih Shen, Gwan Han Wang, Andrew H. J. Chou, Shan Ho
Description	Country affiliation: Taiwan Author Affiliation: Su YC ( Institute of Biochemistry, National Chung-Hsing University, Taichung 40227, Taiwan.)
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 A 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.
File Format	HTM / HTML
ISSN	2053230X
e-ISSN	17443091
DOI	10.1107/S1744309110013941
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Issue Number	Pt 6
Volume Number	66
Language	English
Publisher	Wiley
Publisher Date	2010-06-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Cation Transport Proteins Chemistry Stenotrophomonas Maltophilia Zinc Src Homology Domains Amino Acid Sequence Metabolism Crystallography, X-ray Models, Molecular Molecular Sequence Data Protein Binding Protein Structure, Quaternary Sequence Alignment Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

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