PDBsum entry: 1gmx

Transferase

PDB id: 1gmx

Contents

Protein chain

108 a.a. *

Ligands

ACT ×2

EDO ×7

Waters ×100

* Residue conservation analysis

PDB id:

1gmx

Name:

Transferase

Title:

Escherichia coli glpe sulfurtransferase

Structure:

Glpe protein. Chain: a. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 469008. Strain: bl21(de3). Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.10Å R-factor: 0.128 R-free: 0.151

Authors:

A.Spallarossa,J.T.Donahue,T.J.Larson,M.Bolognesi,D.Bordo

Key ref:

A.Spallarossa et al. (2001). Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily. Structure, 9, 1117-1125. PubMed id: 11709175 DOI: 10.1016/S0969-2126(01)00666-9

Date:

25-Sep-01 Release date: 28-Nov-01

Protein chain

P0A6V5  (GLPE_ECOLI) -  Thiosulfate sulfurtransferase glpE

Seq: 108 a.a.

Struc: 108 a.a.

Enzyme reactions

• Enzyme class: E.C.2.8.1.1 - Thiosulfate sulfurtransferase.
• Reaction: Thiosulfate + cyanide = sulfite + thiocyanate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: cytoplasm (1 term)
• Biological process: glycerol metabolic process (1 term)
• Biochemical function: transferase activity (2 terms)

reference

DOI no: 10.1016/S0969-2126(01)00666-9

Structure 9:1117-1125 (2001)

PubMed id: 11709175

Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily.

A.Spallarossa, J.L.Donahue, T.J.Larson, M.Bolognesi, D.Bordo.

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.

Selected figure(s)

Figure 2.
Figure 2. Stereo Representation of the GlpE Active-Site Loop(a) The active site as observed in native GlpE, with the persulfide sulfur atom (Sd) bound to the Cys65 Sg atom. The electron density map (2F[o]-F[c]) is contoured at 1.0 s. Hydrogen bonds involving Sd in its major conformer are shown as red lines. Hydrogen bonds involving the two water molecules observed in front of the active site are not drawn for clarity. O, N, C, and S atoms are represented in red, blue, black, and yellow, respectively. The two alternate Cys65 conformations are shown in gray and light blue, respectively. The drawing was prepared with BOBSCRIPT [52].(b) Sulfur-free GlpE after soaking with KCN, showing a sodium cation (in magenta) at the center of the active site, bound to the active-site Cys65 thiol group

The above figure is reprinted by permission from Cell Press: Structure (2001, 9, 1117-1125) copyright 2001.

Figure was selected by an automated process.