3UEH

Crystal structure of human Survivin H80A mutant

3UEH の概要

• エントリーDOI: 10.2210/pdb3ueh/pdb
• 関連するPDBエントリー: 3UEC 3UED 3UEE 3UEF 3UEG 3UEI
• 分子名称: Baculoviral IAP repeat-containing protein 5, ZINC ION, 1,2-ETHANEDIOL, ... (6 entities in total)
• 機能のキーワード: zinc finger, bir domain, chromosomal passenger complex, cell division, mitosis, cell cycle
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: O15392
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34073.42

構造登録者

Niedzialkowska, E.,Porebski, P.J.,Wang, F.,Higgins, J.M.,Stukenberg, P.T.,Minor, W. (登録日: 2011-10-30, 公開日: 2012-03-07, 最終更新日: 2023-09-13)

主引用文献

Niedzialkowska, E.,Wang, F.,Porebski, P.J.,Minor, W.,Higgins, J.M.,Stukenberg, P.T.
Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres.
Mol Biol Cell, 23:1457-1466, 2012

PubMed Abstract: Survivin, a subunit of the chromosome passenger complex (CPC), binds the N-terminal tail of histone H3, which is phosphorylated on T3 by Haspin kinase, and localizes the complex to the inner centromeres. We used x-ray crystallography to determine the residues of Survivin that are important in binding phosphomodified histone H3. Mutation of amino acids that interact with the histone N-terminus lowered in vitro tail binding affinity and reduced CPC recruitment to the inner centromere in cells, validating our solved structures. Phylogenetic analysis shows that nonmammalian vertebrates have two Survivin paralogues, which we name class A and B. A distinguishing feature of these paralogues is an H-to-R change in an amino acid that interacts with the histone T3 phosphate. The binding to histone tails of the human class A paralogue, which has a histidine at this position, is sensitive to changes around physiological pH, whereas Xenopus Survivin class B is less so. Our data demonstrate that Survivin paralogues have different characteristics of phosphospecific binding to threonine-3 of histone H3, providing new insight into the biology of the inner centromere.

PubMed: 22357620
DOI: 10.1091/mbc.E11-11-0904

実験手法

X-RAY DIFFRACTION (2.6 Å)