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331 a.a.
 L-glutamine |
+ |
H(2)O |
= |
 L-glutamate |
+ |
NH(3) |
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 L-asparagine |
+ |
H(2)O |
= |
 L-aspartate |
+ |
NH(3) |
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Key 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.
Literature references that cite this PDB file's key reference
PubMed id Reference 19177345 D.E.Tronrud, and B.W.Matthews (2009).
Sorting the chaff from the wheat at the PDB.Protein Sci, 18, 2-5.
15265041 D.Borek, K.Michalska, K.Brzezinski, A.Kisiel, J.Podkowinski, D.T.Bonthron, D.Krowarsch, J.Otlewski, and M.Jaskolski (2004).
Expression, purification and catalytic activity of Lupinus luteus asparagine beta-amidohydrolase and its Escherichia coli homolog.Eur J Biochem, 271, 3215-3226.
8898907 J.Lubkowski, G.J.Palm, G.L.Gilliland, C.Derst, K.H.Röhm, and A.Wlodawer (1996).
Crystal structure and amino acid sequence of Wolinella succinogenes L-asparaginase.Eur J Biochem, 241, 201-207.
PDB code: 1wsa The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.
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