Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4LDV

Crystal structure of the DNA binding domain of A. thailana auxin response factor 1

Summary for 4LDV
Entry DOI10.2210/pdb4ldv/pdb
Related4LDW 4LDx 4LDy
DescriptorAuxin response factor 1, IODIDE ION, CHLORIDE ION, ... (5 entities in total)
Functional Keywordstranscription factor, dna binding, nucleus, transcription
Biological sourceArabidopsis thaliana (mouse-ear cress,thale-cress)
Cellular locationNucleus: Q8L7G0
Total number of polymer chains1
Total formula weight41684.56
Authors
boer, D.R.,Freire-Rios, A.,van den Berg, W.M.A.,Weijers, D.,Coll, M. (deposition date: 2013-06-25, release date: 2014-02-12, Last modification date: 2024-04-03)
Primary citationBoer, D.R.,Freire-Rios, A.,van den Berg, W.A.,Saaki, T.,Manfield, I.W.,Kepinski, S.,Lopez-Vidrieo, I.,Franco-Zorrilla, J.M.,de Vries, S.C.,Solano, R.,Weijers, D.,Coll, M.
Structural Basis for DNA Binding Specificity by the Auxin-Dependent ARF Transcription Factors.
Cell(Cambridge,Mass.), 156:577-589, 2014
Cited by
PubMed Abstract: Auxin regulates numerous plant developmental processes by controlling gene expression via a family of functionally distinct DNA-binding auxin response factors (ARFs), yet the mechanistic basis for generating specificity in auxin response is unknown. Here, we address this question by solving high-resolution crystal structures of the pivotal Arabidopsis developmental regulator ARF5/MONOPTEROS (MP), its divergent paralog ARF1, and a complex of ARF1 and a generic auxin response DNA element (AuxRE). We show that ARF DNA-binding domains also homodimerize to generate cooperative DNA binding, which is critical for in vivo ARF5/MP function. Strikingly, DNA-contacting residues are conserved between ARFs, and we discover that monomers have the same intrinsic specificity. ARF1 and ARF5 homodimers, however, differ in spacing tolerated between binding sites. Our data identify the DNA-binding domain as an ARF dimerization domain, suggest that ARF dimers bind complex sites as molecular calipers with ARF-specific spacing preference, and provide an atomic-scale mechanistic model for specificity in auxin response.
PubMed: 24485461
DOI: 10.1016/j.cell.2013.12.027
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.45 Å)
Structure validation

227344

数据于2024-11-13公开中

PDB statisticsPDBj update infoContact PDBjnumon