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Bacterial amidohydrolase
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PDB id
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1agx
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.3.5.1.38
- Glutamin-(asparagin-)ase.
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Reaction:
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1.
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L-glutamine + H2O = L-glutamate + NH3
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2.
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L-asparagine + H2O = L-aspartate + NH3
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L-glutamine
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+
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H(2)O
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=
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L-glutamate
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+
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NH(3)
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L-asparagine
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+
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H(2)O
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=
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L-aspartate
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+
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NH(3)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Cellular component
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periplasmic space
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1 term
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Biological process
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cellular amino acid metabolic process
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2 terms
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Biochemical function
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hydrolase activity
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3 terms
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DOI no:
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Acta Crystallogr D Biol Crystallogr
50:826-832
(1994)
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PubMed id:
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Refined crystal structure of Acinetobacter glutaminasificans glutaminase-asparaginase.
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J.Lubkowski,
A.Wlodawer,
D.Housset,
I.T.Weber,
H.L.Ammon,
K.C.Murphy,
A.L.Swain.
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ABSTRACT
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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.
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Selected figure(s)
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Figure 1.
Fig. 1. The AGA tetramer. Each subunit of the 222 symmetric
molecule is colored differently. The spheres indicate active-site
locations.
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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.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1994,
50,
826-832)
copyright 1994.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.E.Tronrud,
and
B.W.Matthews
(2009).
Sorting the chaff from the wheat at the PDB.
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Protein Sci, 18,
2-5.
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P.Dhavala,
J.Krasotkina,
C.Dubreuil,
and
A.C.Papageorgiou
(2008).
Expression, purification and crystallization of Helicobacter pylori L-asparaginase.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 64,
740-742.
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M.K.Yun,
A.Nourse,
S.W.White,
C.O.Rock,
and
R.J.Heath
(2007).
Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase I.
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J Mol Biol, 369,
794-811.
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PDB codes:
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E.Schmitt,
M.Panvert,
S.Blanquet,
and
Y.Mechulam
(2005).
Structural basis for tRNA-dependent amidotransferase function.
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Structure, 13,
1421-1433.
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PDB code:
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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.
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Eur J Biochem, 271,
3215-3226.
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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.
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Eur J Biochem, 241,
201-207.
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PDB code:
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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
codes are
shown on the right.
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