4QR9

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

4QR9 の概要

• エントリーDOI: 10.2210/pdb4qr9/pdb
• 分子名称: High mobility group protein B1, DNA (5'-D(*AP*TP*AP*TP*CP*GP*AP*TP*AP*T)-3'), MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: hmg-box, hmgb1, box a domain, high mobility group, dna-binding, bend dna, kink dna, architectural factor, minor groove, chromatin, nucleus, dna binding protein
• 由来する生物種: Rattus norvegicus (brown rat,rat,rats); 詳細
• 細胞内の位置: Nucleus: P63159
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 30095.03

構造登録者

Sanchez-Giraldo, R.,Acosta-Reyes, F.J.,Malarkey, C.S.,Saperas, N.,Churchill, M.E.A.,Campos, J.L. (登録日: 2014-06-30, 公開日: 2015-07-01, 最終更新日: 2024-10-09)

主引用文献

Sanchez-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

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

実験手法

X-RAY DIFFRACTION (2 Å)