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PDBsum entry 1xaa
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Oxidoreductase
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PDB id
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1xaa
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References listed in PDB file
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Key reference
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Title
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Cryocrystallography of 3-Isopropylmalate dehydrogenase from thermus thermophilus and its chimeric enzyme.
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Authors
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C.Nagata,
H.Moriyama,
N.Tanaka,
M.Nakasako,
M.Yamamoto,
T.Ueki,
T.Oshima.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1996,
52,
623-630.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Abstract
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The crystal structures of thermostable enzyme, 3-isopropylmalate dehydrogenase
of Thermus thermophilus (10T) and a chimeric enzyme between T. thermophilus and
Bacillus subtilus with one point mutation (cS82R), were determined at both 100
and 150 K. At the cryogenic condition, the volume of the unit cell decreased by
5% as a result of a contraction in the solvent region. Although the overall
structures of both enzymes at low temperature were the same as that of 10T at
room temperature, interactions between two domains and between two subunits in a
functional dimer of cS82R were significantly altered. The decrease in the
average temperature factor of 10T at low temperature and no significant decrease
for cS82R suggested that the structure of the engineered enzyme (cS82R) may have
many conformational substates even at low temperature, while the native enzyme
(10T) at low temperature has a more definite conformation than that at room
temperature. The location of water molecules around the enzyme molecule and the
calculation of the radii of gyration suggested that cS82R had a weaker hydration
than 10T.
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Figure 6.
Fig. 6. The temperature factors of the amino-acid residues. The solid
lines indicate those at 100 K and the dotted lines indicate those at
293 K. (a) 10T. (b) cS82R.
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Figure 7.
Fig. 7. Histogram of the hydrogenbond distance beteen acceptor and
donor within 2.4 and 3.4 A for 0T (gray bars) and cS82R (white
bars). (a) The proteinprotein interaction. (b) The proteinwater
interaction. (c) The waterwater interacton.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1996,
52,
623-630)
copyright 1996.
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Secondary reference #1
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Title
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Purification, Catalytic properties, And thermal stability of threo-Ds-3-Isopropylmalate dehydrogenase coded by leub gene from an extreme thermophile, Thermus thermophilus strain hb8.
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Authors
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T.Yamada,
N.Akutsu,
K.Miyazaki,
K.Kakinuma,
M.Yoshida,
T.Oshima.
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Ref.
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J Biochem (tokyo), 1990,
108,
449-456.
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PubMed id
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