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

4QR9

Crystal structure of two HMGB1 Box A domains cooperating to underwind and kink a DNA

Summary for 4QR9
Entry DOI10.2210/pdb4qr9/pdb
DescriptorHigh mobility group protein B1, DNA (5'-D(*AP*TP*AP*TP*CP*GP*AP*TP*AP*T)-3'), MAGNESIUM ION, ... (4 entities in total)
Functional Keywordshmg-box, hmgb1, box a domain, high mobility group, dna-binding, bend dna, kink dna, architectural factor, minor groove, chromatin, nucleus, dna binding protein
Biological sourceRattus norvegicus (brown rat,rat,rats)
More
Cellular locationNucleus: P63159
Total number of polymer chains6
Total formula weight30095.03
Authors
Sanchez-Giraldo, R.,Acosta-Reyes, F.J.,Malarkey, C.S.,Saperas, N.,Churchill, M.E.A.,Campos, J.L. (deposition date: 2014-06-30, release date: 2015-07-01, Last modification date: 2024-10-09)
Primary citationSanchez-Giraldo, R.,Acosta-Reyes, F.J.,Malarkey, C.S.,Saperas, N.,Churchill, M.E.,Campos, J.L.
Two high-mobility group box domains act together to underwind and kink DNA.
Acta Crystallogr.,Sect.D, 71:1423-1432, 2015
Cited by
PubMed Abstract: High-mobility group protein 1 (HMGB1) is an essential and ubiquitous DNA architectural factor that influences a myriad of cellular processes. HMGB1 contains two DNA-binding domains, box A and box B, which have little sequence specificity but have remarkable abilities to underwind and bend DNA. Although HMGB1 box A is thought to be responsible for the majority of HMGB1-DNA interactions with pre-bent or kinked DNA, little is known about how it recognizes unmodified DNA. Here, the crystal structure of HMGB1 box A bound to an AT-rich DNA fragment is reported at a resolution of 2 Å. Two box A domains of HMGB1 collaborate in an unusual configuration in which the Phe37 residues of both domains stack together and intercalate the same CG base pair, generating highly kinked DNA. This represents a novel mode of DNA recognition for HMGB proteins and reveals a mechanism by which structure-specific HMG boxes kink linear DNA.
PubMed: 26143914
DOI: 10.1107/S1399004715007452
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon