4CA9

Structure of the Nucleoplasmin-like N-terminal domain of Drosophila FKBP39

4CA9 の概要

• エントリーDOI: 10.2210/pdb4ca9/pdb
• NMR情報: BMRB: 19541
• 分子名称: 39 KDA FK506-BINDING NUCLEAR PROTEIN (1 entity in total)
• 機能のキーワード: isomerase, proline isomerase, nucleoplasmin, histone chaperone
• 由来する生物種: DROSOPHILA MELANOGASTER (FRUIT FLY)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 54102.05

構造登録者

Artero, J.,Forsyth, T.,Callow, P.,Watson, A.A.,Zhang, W.,Laue, E.D.,Edlich-Muth, C.,Przewloka, M. (登録日: 2013-10-07, 公開日: 2014-10-29, 最終更新日: 2024-06-19)

主引用文献

Edlich-Muth, C.,Artero, J.,Callow, P.,Przewloka, M.R.,Watson, A.A.,Zhang, W.,Glover, D.M.,Debski, J.,Dadlez, M.,Round, A.R.,Trevor Forsyth, V.,Laue, E.D.
The Pentameric Nucleoplasmin Fold is Present in Drosophila Fkbp39 and a Large Number of Chromatin-Related Proteins.
J.Mol.Biol., 427:1949-, 2015

PubMed Abstract: Nucleoplasmin is a histone chaperone that consists of a pentameric N-terminal domain and an unstructured C-terminal tail. The pentameric core domain, a doughnut-like structure with a central pore, is only found in the nucleoplasmin family. Here, we report the first structure of a nucleoplasmin-like domain (NPL) from the unrelated Drosophila protein, FKBP39, and we present evidence that this protein associates with chromatin. Furthermore, we show that two other chromatin proteins, Arabidopsis thaliana histone deacetylase type 2 (HD2) and Saccharomyces cerevisiae Fpr4, share the NPL fold and form pentamers, or a dimer of pentamers in the case of HD2. Thus, we propose a new family of proteins that share the pentameric nucleoplasmin-like NPL domain and are found in protists, fungi, plants and animals.

PubMed: 25813344
DOI: 10.1016/J.JMB.2015.03.010

実験手法

SOLUTION NMR