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PDBsum entry 1art
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Transferase(aminotransferase)
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PDB id
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1art
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References listed in PDB file
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Key reference
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Title
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X-Ray crystallographic study of pyridoxal 5'-Phosphate-Type aspartate aminotransferases from escherichia coli in open and closed form.
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Authors
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A.Okamoto,
T.Higuchi,
K.Hirotsu,
S.Kuramitsu,
H.Kagamiyama.
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Ref.
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J Biochem (tokyo), 1994,
116,
95.
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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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We determined the three-dimensional structures of aspartate aminotransferase
(AspAT) from Escherichia coli and its complex with inhibitor
(2-methyl-L-aspartate) at 1.8A resolution. This enzyme reversibly catalyzes the
transamination reaction and is a dimer of two identical subunits. Each subunit
has 396 amino acid residues and one pyridoxal 5'-phosphate as a cofactor, and is
divided into two domains, one large and the other small. Upon binding of the
inhibitor, the small domain rotates by 5 degrees toward the large domain to
close the active site. This domain movement is caused mainly by small but
important main-chain conformational changes in the residues located over the
domain interface of the small domain. In chicken mitochondrial AspAT, the domain
movement was larger, with a rotational angle of 13 degrees. By comparison of
these two structures, the difference in the rotational angles was found to be
caused by the larger opening of the domain in the open form of chicken
mitochondrial AspAT. Although the overall structures of these two enzymes were
almost identical, the surface area of the domain interface in the E. coli enzyme
was larger than that in mitochondrial AspAT, suggesting that the structure of
the domain interface is responsible for the degree of movement of the small
domain.
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Secondary reference #1
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Title
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Sequence-Specific 1h nmr assignment and secondary structure of the arc repressor of bacteriophage p22, As determined by two-Dimensional 1h nmr spectroscopy.
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Authors
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J.N.Breg,
R.Boelens,
A.V.George,
R.Kaptein.
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Ref.
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Biochemistry, 1989,
28,
9826-9833.
[DOI no: ]
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PubMed id
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