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PDBsum entry 1ltp
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Transcription regulation
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PDB id
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1ltp
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References listed in PDB file
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Key reference
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Title
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Model of lactose repressor core based on alignment with sugar-Binding proteins is concordant with genetic and chemical data.
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Authors
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J.C.Nichols,
N.K.Vyas,
F.A.Quiocho,
K.S.Matthews.
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Ref.
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J Biol Chem, 1993,
268,
17602-17612.
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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
percentage match of
92%.
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Abstract
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Using primary sequence similarity to arabinose-binding protein,
D-glucose/D-galactose-binding protein, and ribose-binding protein (Vyas, N. K.,
Vyas, M. N., and Quiocho, F. A. (1991) J. Biol. Chem. 266, 5226-5237; Mowbray,
S. L., and Cole, L. B. (1992) J. Mol. Biol. 225, 155-175), the core domain
(residues 62-323) of the bacterial regulatory protein lac repressor has been
aligned to these sugar-binding proteins of known structure. Although the
sequence identity is not striking, there is strong overall homology based on two
separate matrix scoring systems (minimum base change per codon (MBC/C) and amino
acid homology per residue (AAH/R)) (mean score: MBC/C < 1.25, AAH/R >
5.50; random sequences: MBC/C = 1.45, AAH/R = 4.46). Similarly, the predicted
secondary structure of the repressor exhibits excellent agreement with the known
secondary structures of the sugar-binding proteins. Using this primary sequence
alignment, the tertiary structure of the core domain of the lac repressor has
been modeled based on the known structures of the sugar-binding proteins as
templates. While the structure deduced for the repressor is hypothetical, the
model generated allows a comparison between the predicted tertiary arrangement
and the wealth of genetic and chemical data elucidated for the repressor.
Important residues involved in operator and sugar binding and in protein
assembly have been identified using genetic methods, and placement of these
residues in the model is consistent with their known function. This approach,
therefore, provides a means to visualize the core domain of the lac repressor
that allows interpretation of genetic and chemical data for specific residues
and rational design of future experiments.
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Secondary reference #1
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Title
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Comparison of the periplasmic receptors for l-Arabinose, D-Glucose/d-Galactose, And d-Ribose. Structural and functional similarity.
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Authors
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N.K.Vyas,
M.N.Vyas,
F.A.Quiocho.
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Ref.
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J Biol Chem, 1991,
266,
5226-5237.
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PubMed id
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