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PDBsum entry 2zc0
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References listed in PDB file
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Key reference
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Title
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Structure of an archaeal alanine:glyoxylate aminotransferase.
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Authors
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H.Sakuraba,
K.Yoneda,
K.Takeuchi,
H.Tsuge,
N.Katunuma,
T.Ohshima.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2008,
64,
696-699.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of a novel alanine:glyoxylate aminotransferase from the
hyperthermophilic archaeon Thermococcus litoralis was determined at 2.3 A
resolution. The asymmetric unit contains four homologous subunits and the
functional tetramer is generated by noncrystallographic 222 symmetry. Although
the main-chain coordinates of the monomer of the Thermococcus litoralis enzyme
showed a high degree of similarity to those of aspartate aminotransferase from
Thermus thermophilus HB8, the amino-acid residues involved in substrate binding
in the aspartate aminotransferase are only partially conserved in the
Thermococcus litoralis enzyme. This may account for the difference in the
substrate specificities of the two enzymes.
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Figure 2.
Figure 2 Stereographic close-up of the substrate-binding site.
The structure of Tc. litoralis AGT (green) is superimposed on
that of Tm. thermophilus AspAT (yellow). The maleate molecule is
shown as a stick model in cyan. The putative interactions are
shown by dotted lines. N and O atoms are shown in blue and red,
respectively.
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2008,
64,
696-699)
copyright 2008.
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