2H4R

Crystal structure of wildtype MENT in the native conformation

2H4R の概要

• エントリーDOI: 10.2210/pdb2h4r/pdb
• 関連するPDBエントリー: 2H4P 2H4Q 2H4S
• 分子名称: Heterochromatin-associated protein MENT (2 entities in total)
• 機能のキーワード: serine protease inhibitor, serpin, hydrolase inhibitor
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Nucleus: O73790
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48029.28

構造登録者

Irving, J.A.,Whisstock, J.C.,Buckle, A.M.,McGowan, S. (登録日: 2006-05-25, 公開日: 2006-07-18, 最終更新日: 2024-11-20)

主引用文献

McGowan, S.,Buckle, A.M.,Irving, J.A.,Ong, P.C.,Bashtannyk-Puhalovich, T.A.,Kan, W.T.,Henderson, K.N.,Bulynko, Y.A.,Popova, E.Y.,Smith, A.I.,Bottomley, S.P.,Rossjohn, J.,Grigoryev, S.A.,Pike, R.N.,Whisstock, J.C.
X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation.
Embo J., 25:3144-3155, 2006

PubMed Abstract: Most serpins are associated with protease inhibition, and their ability to form loop-sheet polymers is linked to conformational disease and the human serpinopathies. Here we describe the structural and functional dissection of how a unique serpin, the non-histone architectural protein, MENT (Myeloid and Erythroid Nuclear Termination stage-specific protein), participates in DNA and chromatin condensation. Our data suggest that MENT contains at least two distinct DNA-binding sites, consistent with its simultaneous binding to the two closely juxtaposed linker DNA segments on a nucleosome. Remarkably, our studies suggest that the reactive centre loop, a region of the MENT molecule essential for chromatin bridging in vivo and in vitro, is able to mediate formation of a loop-sheet oligomer. These data provide mechanistic insight into chromatin compaction by a non-histone architectural protein and suggest how the structural plasticity of serpins has adapted to mediate physiological, rather than pathogenic, loop-sheet linkages.

PubMed: 16810322
DOI: 10.1038/sj.emboj.7601201

実験手法

X-RAY DIFFRACTION (2.7 Å)