1AGX

REFINED CRYSTAL STRUCTURE OF ACINETOBACTER GLUTAMINASIFICANS GLUTAMINASE-ASPARAGINASE

Summary for 1AGX

• Entry DOI: 10.2210/pdb1agx/pdb
• Descriptor: GLUTAMINASE-ASPARAGINASE (1 entity in total)
• Functional Keywords: bacterial amidohydrolase
• Biological source: Acinetobacter glutaminasificans
• Total number of polymer chains: 1
• Total formula weight: 35523.35

Authors

Lubkowski, J.,Wlodawer, A.,Housset, D.,Weber, I.T.,Ammon, H.L.,Murphy, K.C.,Swain, A.L. (deposition date: 1994-07-13, release date: 1994-12-20, Last modification date: 2024-02-07)

Primary citation

Lubkowski, J.,Wlodawer, A.,Housset, D.,Weber, I.T.,Ammon, H.L.,Murphy, K.C.,Swain, A.L.
Refined crystal structure of Acinetobacter glutaminasificans glutaminase-asparaginase.
Acta Crystallogr.,Sect.D, 50:826-832, 1994

PubMed 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.

PubMed: 15299349
DOI: 10.1107/S0907444994003446

Experimental method

X-RAY DIFFRACTION (2.9 Å)