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PDBsum entry 3a5t
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Transcription regulator/DNA
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PDB id
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3a5t
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References listed in PDB file
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Key reference
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Title
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Structural basis of alternative DNA recognition by maf transcription factors.
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Authors
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H.Kurokawa,
H.Motohashi,
S.Sueno,
M.Kimura,
H.Takagawa,
Y.Kanno,
M.Yamamoto,
T.Tanaka.
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Ref.
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Mol Cell Biol, 2009,
29,
6232-6244.
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PubMed id
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Abstract
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Maf transcription factors constitute a family of the basic region-leucine zipper
(bZip) factors and recognize unusually long DNA motifs (13 or 14 bp), termed the
Maf recognition element (MARE). The MARE harbors extended GC sequences on each
side of its core motif, which is similar to TRE or CRE (7 or 8 bp) recognized by
the AP1 and CREB/ATF families, respectively. To ascertain the structural basis
governing the acquirement of such unique DNA recognition, we determined the
crystal structure of the MafG-DNA complex. Each MafG monomer consists of three
helices in which the carboxyl-terminal long helix organizes one DNA-contacting
element and one coiled-coil dimer formation element. To our surprise, two
well-conserved residues, Arg57 and Asn61 in the basic region, play critical
roles in Maf-specific DNA recognition. These two residues show unique side-chain
orientations and interact directly with the extended GC bases. Maf-specific
residues in the amino-terminal and basic regions appear to indirectly stabilize
MARE recognition through DNA backbone phosphate interactions. This study
revealed an alternative DNA recognition mechanism of the bZip factors that
bestows specific target gene profiles upon Maf homodimers or Maf-containing
heterodimers.
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