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2KFK

Solution structure of Bem1p PB1 domain complexed with Cdc24p PB1 domain

2KFK の概要
エントリーDOI10.2210/pdb2kfk/pdb
分子名称Bud emergence protein 1, Cell division control protein 24 (2 entities in total)
機能のキーワードpb1, budding, yeast, phox, signaling protein
由来する生物種Saccharomyces cerevisiae (yeast)
詳細
細胞内の位置Cytoplasm, cytoskeleton: P29366
タンパク質・核酸の鎖数2
化学式量合計19030.78
構造登録者
Kobashigawa, Y.,Yoshinaga, S.,Tandai, T.,Ogura, K.,Inagaki, F. (登録日: 2009-02-23, 公開日: 2009-10-06, 最終更新日: 2024-05-29)
主引用文献Ogura, K.,Tandai, T.,Yoshinaga, S.,Kobashigawa, Y.,Kumeta, H.,Ito, T.,Sumimoto, H.,Inagaki, F.
NMR structure of the heterodimer of Bem1 and Cdc24 PB1 domains from Saccharomyces cerevisiae
J.Biochem., 146:317-325, 2009
Cited by
PubMed Abstract: Bem1 and Cdc24 of the budding yeast Saccharomyces cerevisiae interact with each other through PB1-PB1 heterodimer formation to regulate the establishment of cell polarity. Here we present the tertiary structure of the heterodimer of Bem1 and Cdc24 PB1 domains determined by NMR spectroscopy. To avoid ambiguity in the NMR spectral analysis, we first prepared a mutant of the Cdc24 PB1 domain that had truncated loops. The mutant provided well dispersed spectra without spectral overlapping, thus allowing unambiguous spectral assignments for structure determination. We confirmed that the loop deletion-mutant was quite similar to the wild-type in both 3D structure and binding affinity. The NMR structure of the heterodimer of the deletion-mutant of Cdc24 PB1 and Bem1 PB1 was determined using a variety of isotope labelled samples including perdeuteration. The interface between the Bem1/Cdc24 PB1 heterodimer was analysed at atomic resolution. Through a comparison with the tertiary structures of other PB1-PB1 heterodimers, we found that conserved electrostatic properties on the molecular surface were commonly used for PB1-PB1 interaction, but hydrophobic interactions were important for cognate interaction in Bem1/Cdc24 PB1 heterodimer formation.
PubMed: 19451149
DOI: 10.1093/jb/mvp075
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2kfk
検証レポート(詳細版)ダウンロードをダウンロード

248636

件を2026-02-04に公開中

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