4AUW

CRYSTAL STRUCTURE OF THE BZIP HOMODIMERIC MAFB IN COMPLEX WITH THE C- MARE BINDING SITE

Summary for 4AUW

• Entry DOI: 10.2210/pdb4auw/pdb
• Descriptor: TRANSCRIPTION FACTOR MAFB, C-MARE BINDING SITE (5'-D(*AP*TP*AP*AP*TP*GP*CP*TP* GP*AP*CP*GP*TP*CP*AP*GP*CP*AP*AP*TP*T)-3'), MERCURY (II) ION, ... (5 entities in total)
• Functional Keywords: transcription, dna, macrophage
• Biological source: MUS MUSCULUS (HOUSE MOUSE); More
• Cellular location: Nucleus : P54841
• Total number of polymer chains: 8
• Total formula weight: 72884.38

Authors

Textor, L.C.,Holton, S.,Wilmanns, M. (deposition date: 2012-05-22, release date: 2013-06-05, Last modification date: 2024-05-08)

Primary citation

Textor, L.C.,Wilmanns, M.,Holton, S.J.
Expression, purification, crystallization and preliminary crystallographic analysis of the mouse transcription factor MafB in complex with its DNA-recognition motif Cmare
Acta Crystallogr Sect F Struct Biol Cryst Commun., 63:657-661, 2007

PubMed Abstract: The MafB transcription factor (residues 211-305) has been overexpressed in and purified from Escherichia coli. A protein-DNA complex between the MafB homodimer and the 21 bp Maf-recognition sequence known as Cmare has been successfully reconstituted in vitro and subsequently crystallized. The diffraction properties of the protein-DNA complex crystals were improved using a combination of protein-construct boundary optimization and targeted mutagenesis to promote crystal lattice stability. Both native and mercury-derivatized crystals have been prepared using these optimized conditions. The crystals belong to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 94.8, c = 197.9 A. An anomalous difference Patterson map computed using data collected from crystals grown in the presence of HgCl(2) reveals four peaks. This corresponds to two copies of the protein-DNA complex in the asymmetric unit, with a solvent content of 62% and a Matthews coefficient of 3.22 A(3) Da(-1).

PubMed: 17671361
DOI: 10.1107/S1744309107031260

Experimental method

X-RAY DIFFRACTION (2.9 Å)