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3A5T

Crystal structure of MafG-DNA complex

Summary for 3A5T
Entry DOI10.2210/pdb3a5t/pdb
DescriptorTranscription factor MafG, 5'-D(*CP*TP*GP*AP*TP*GP*AP*GP*TP*CP*AP*GP*CP*AP*C)-3', 5'-D(*GP*TP*GP*CP*TP*GP*AP*CP*TP*CP*AP*TP*CP*AP*G)-3', ... (5 entities in total)
Functional Keywordsprotein-dna complex, bzip factor, acetylation, dna-binding, isopeptide bond, nucleus, repressor, transcription, transcription regulation, ubl conjugation, transcription regulator-dna complex, transcription regulator/dna
Biological sourceMus musculus (mouse)
More
Cellular locationNucleus : O54790
Total number of polymer chains4
Total formula weight34246.98
Authors
Kurokawa, H.,Motohashi, H.,Sueno, S.,Kimura, M.,Takagawa, H.,Kanno, Y.,Yamamoto, M.,Tanaka, T. (deposition date: 2009-08-11, release date: 2009-10-13, Last modification date: 2024-10-23)
Primary citationKurokawa, H.,Motohashi, H.,Sueno, S.,Kimura, M.,Takagawa, H.,Kanno, Y.,Yamamoto, M.,Tanaka, T.
Structural Basis of Alternative DNA Recognition by Maf Transcription Factors
Mol.Cell.Biol., 29:6232-6244, 2009
Cited by
PubMed Abstract: 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.
PubMed: 19797082
DOI: 10.1128/MCB.00708-09
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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数据于2025-06-18公开中

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