PDBsum entry: 1agx

Bacterial amidohydrolase

PDB id: 1agx

Contents

Protein chain

331 a.a. *

* Residue conservation analysis

PDB id:

1agx

Name:

Bacterial amidohydrolase

Title:

Refined crystal structure of acinetobacter glutaminasificans glutaminase-asparaginase

Structure:

Glutaminase-asparaginase. Chain: a. Engineered: yes

Source:

Acinetobacter glutaminasificans. Organism_taxid: 474

Biol. unit:

Tetramer (from PQS)

Resolution:

2.90Å R-factor: 0.171

Authors:

J.Lubkowski,A.Wlodawer,D.Housset,I.T.Weber,H.L.Ammon,K.C.Mur A.L.Swain

Key ref:

J.Lubkowski et al. (1994). Refined crystal structure of Acinetobacter glutaminasificans glutaminase-asparaginase. Acta Crystallogr D Biol Crystallogr, 50, 826-832. PubMed id: 15299349 DOI: 10.1107/S0907444994003446

Date:

13-Jul-94 Release date: 20-Dec-94

Protein chain

P10172  (ASPQ_ACIGL) -  Glutaminase-asparaginase

Seq: 331 a.a.

Struc: 331 a.a.

Enzyme reactions

• Enzyme class: E.C.3.5.1.38 - Glutamin-(asparagin-)ase.
• Reaction:
  1. L-glutamine + H₂O = L-glutamate + NH₃
  2. L-asparagine + H₂O = L-aspartate + NH₃

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

 Gene Ontology (GO) functional annotation 

• Cellular component: periplasmic space (1 term)
• Biological process: cellular amino acid metabolic process (2 terms)
• Biochemical function: hydrolase activity (3 terms)

reference

DOI no: 10.1107/S0907444994003446

Acta Crystallogr D Biol Crystallogr 50:826-832 (1994)

PubMed id: 15299349

Refined crystal structure of Acinetobacter glutaminasificans glutaminase-asparaginase.

J.Lubkowski, A.Wlodawer, D.Housset, I.T.Weber, H.L.Ammon, K.C.Murphy, A.L.Swain.

ABSTRACT

The crystal structure of glutaminase-asparaginase from Acinetobacter glutaminasificans has been reinterpreted and refined to an R factor of 0.171 at 2.9 A resolution, using the same X-ray diffraction data that were used to build a preliminary model of this enzyme [Ammon, Weber, Wlodawer, Harrison, Gilliland, Murphy, Sjölin & Roberts (1988). J. Biol. Chem. 263, 150-156]. The current model, which does not include solvent, is based in part on the related structure of Escherichia coli asparaginase and is significantly different from the structure of the enzyme from A. glutaminasificans described previously. The reason for the discrepancies has been traced to insufficient phasing power of the original heavy-atom derivative data, which could not be compensated for fully by electron-density modification techniques. The corrected structure of A. glutaminasificans glutaminase-asparaginase is presented and compared with the preliminary model and with the structure of E. coli asparaginase.

Selected figure(s)

Figure 1.
Fig. 1. The AGA tetramer. Each subunit of the 222 symmetric molecule is colored differently. The spheres indicate active-site locations.

Figure 4.
Fig. 4. Ribbon diagram of a subunit of AGA94, illustrating the agreement with AGA88. Brown represents fragments of AGA94 that match the topology and directionality of AGA88; yellow represents fragments of AGA94 for which the topology in AGA88 was identified correctly but the directionality was incorrect; blue represents regions that lack any topological relationship between AGA94 and AGA88.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1994, 50, 826-832) copyright 1994.

Figures were selected by an automated process.