PDBsum entry: 2iuy

Transferase

PDB-id: 2iuy

Biological unit = asymmetric unit, as shown
(as defined in PDB file)

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Description

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References

PROCHECK

Protein chains

340 a.a. *

Ligands

MES ×2

SO4 ×2

Waters ×440

* Residue conservation analysis

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Clefts Calculation

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PDB id:

2iuy

Name:

Transferase

Title:

Crystal structure of avigt4, a glycosyltransferase involved in avilamycin a biosynthesis

Structure:

Glycosyltransferase. Chain: a, b. Synonym: avigt4. Engineered: yes

Source:

Streptomyces viridochromogenes. Organism_taxid: 1938. Expressed in: escherichia coli. Expression_system_taxid: 469008. Other_details: dsm 40721

Biological unit:

Monomer (from PDB file)

UniProt:

Chains A, B: Q93KV2 (Q93KV2_STRVR)

Seq:

Struc:

Seq:

342 a.a.

Struc:

340 a.a.

Key:

PfamA domain

Secondary structure

Resolution:

2.1Å

R-factor:

0.173

R-free:

0.233

Authors:

C.Martinez-Fleites,M.Proctor,S.Roberts,D.N.Bolam, H.J.Gilbert,G.J.Davies

Key ref:

C.Martinez-Fleites et al. (2006). Insights into the synthesis of lipopolysaccharide and antibiotics through the structures of two retaining glycosyltransferases from family GT4.. Chem Biol, 13, 1143-1152. [PubMed id: 17113996] [DOI: 10.1016/j.chembiol.2006.09.005]

Date:

08-Jun-06

Release date:

11-Oct-06

Related entries:

2iv3 crystal structure of avigt4, a glycosyltransferase involved in avilamycin a biosynthesis

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Clefts

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Key reference

DOI no: 10.1016/j.chembiol.2006.09.005

Chem Biol 13:1143-1152 (2006)

PubMed id: 17113996

Insights into the synthesis of lipopolysaccharide and antibiotics through the structures of two retaining glycosyltransferases from family GT4.

C.Martinez-Fleites, M.Proctor, S.Roberts, D.N.Bolam, H.J.Gilbert, G.J.Davies.

ABSTRACT

Glycosyltransferases (GTs) catalyze the synthesis of the myriad glycoconjugates that are central to life. One of the largest families is GT4, which contains several enzymes of therapeutic significance, exemplified by WaaG and AviGT4. WaaG catalyses a key step in lipopolysaccharide synthesis, while AviGT4, produced by Streptomyces viridochromogenes, contributes to the synthesis of the antibiotic avilamycin A. Here we present the crystal structure of both WaaG and AviGT4. The two enzymes contain two "Rossmann-like" (beta/alpha/beta) domains characteristic of the GT-B fold. Both recognition of the donor substrate and the catalytic machinery is similar to other retaining GTs that display the GT-B fold. Structural information is discussed with respect to the evolution of GTs and the therapeutic significance of the two enzymes.

Selected figure(s)

Figure 1.
Figure 1. The Catalytic Action of Two Family GT4 GTs
(A) Schematic diagram of E. coli LPS. GlcN, D-glucosamine; Hep, L-glycero-D-manno-heptose; P, phosphate; EtNP, 2-aminoethyl phosphate; Glc, D-glucose; Gal, D-galactose. WaaG is responsible for the addition of the first glucose moiety via an α-1,3 glycosidic linkage to Hep II.
(B) Structure of the antibiotic avilamycin A. Disruption of the avigt4 gene results in a product lacking the eurekanate moiety (boxed) normally bonded to the L-lyxose residue [8].

Figure 5.
Figure 5. Electrostatic Surface Figures of WaaG and AviGT4
Surface representation of (A) WaaG and (B) AviGT4 colored by electrostatic potential (red, −3kT; blue +3kT, where k is the Boltzmann constant and T is temperature), calculated by the Adaptive Poisson-Boltzmann Solver (APBS) program [44] and visualized with Pymol (DeLano Scientific LLC, http://pymol.sourceforge.net/); ligands are shown in licorice representation.

The above figures are reprinted by permission from Cell Press: Chem Biol (2006, 13, 1143-1152) copyright 2006.

Figures were selected by an automated process.