title: Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily.
abstract: BACKGROUND
  Rhodanese domains are structural modules occurring in the three major evolutionary phyla. They are found as single-domain proteins, as tandemly repeated modules in which the C-terminal domain only bears the properly structured active site, or as members of multidomain proteins. Although in vitro assays show sulfurtransferase or phosphatase activity associated with rhodanese or rhodanese-like domains, specific biological roles for most members of this homology superfamily have not been established.
  
  
  RESULTS
  Eight ORFs coding for proteins consisting of (or containing) a rhodanese domain bearing the potentially catalytic Cys have been identified in the Escherichia coli K-12 genome. One of these codes for the 12-kDa protein GlpE, a member of the sn-glycerol 3-phosphate (glp) regulon. The crystal structure of GlpE, reported here at 1.06 A resolution, displays alpha/beta topology based on five beta strands and five alpha helices. The GlpE catalytic Cys residue is persulfurated and enclosed in a structurally conserved 5-residue loop in a region of positive electrostatic field.
  
  
  CONCLUSIONS
  Relative to the two-domain rhodanese enzymes of known three-dimensional structure, GlpE displays substantial shortening of loops connecting alpha helices and beta sheets, resulting in radical conformational changes surrounding the active site. As a consequence, GlpE is structurally more similar to Cdc25 phosphatases than to bovine or Azotobacter vinelandii rhodaneses. Sequence searches through completed genomes indicate that GlpE can be considered to be the prototype structure for the ubiquitous single-domain rhodanese module.
authors.affiliation: Department of Pharmaceutical Sciences, University of Genova, Viale Benedetto XV, 3, 16132, Genova, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Spallarossa
authors.forename: J L
authors.initials: JL
authors.lastname: Donahue
authors.forename: T J
authors.initials: TJ
authors.lastname: Larson
authors.forename: M
authors.initials: M
authors.lastname: Bolognesi
authors.forename: D
authors.initials: D
authors.lastname: Bordo
mesh_terms: D000595:Amino Acid Sequence; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry*; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D005810:Multigene Family; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013466:Sulfurtransferases / Q000737:chemistry; D013884:Thiosulfate Sulfurtransferase / Q000737:chemistry*
chemical_list: D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C102897:GlpE protein, E coli; D013466:Sulfurtransferases; D013884:Thiosulfate Sulfurtransferase