4WPE

Crystal Structure of Hof1p F-BAR domain

4WPE の概要

• エントリーDOI: 10.2210/pdb4wpe/pdb
• 分子名称: Cytokinesis protein 2 (2 entities in total)
• 機能のキーワード: f-bar domain, membrane, protein binding
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Cytoplasm, cytoskeleton: Q05080
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36095.10

構造登録者

Lemmon, M.A.,Moravcevic, K. (登録日: 2014-10-17, 公開日: 2014-12-24, 最終更新日: 2024-11-13)

主引用文献

Moravcevic, K.,Alvarado, D.,Schmitz, K.R.,Kenniston, J.A.,Mendrola, J.M.,Ferguson, K.M.,Lemmon, M.A.
Comparison of Saccharomyces cerevisiae F-BAR Domain Structures Reveals a Conserved Inositol Phosphate Binding Site.
Structure, 23:352-363, 2015

PubMed Abstract: F-BAR domains control membrane interactions in endocytosis, cytokinesis, and cell signaling. Although they are generally thought to bind curved membranes containing negatively charged phospholipids, numerous functional studies argue that differences in lipid-binding selectivities of F-BAR domains are functionally important. Here, we compare membrane-binding properties of the Saccharomyces cerevisiae F-BAR domains in vitro and in vivo. Whereas some F-BAR domains (such as Bzz1p and Hof1p F-BARs) bind equally well to all phospholipids, the F-BAR domain from the RhoGAP Rgd1p preferentially binds phosphoinositides. We determined X-ray crystal structures of F-BAR domains from Hof1p and Rgd1p, the latter bound to an inositol phosphate. The structures explain phospholipid-binding selectivity differences and reveal an F-BAR phosphoinositide binding site that is fully conserved in a mammalian RhoGAP called Gmip and is partly retained in certain other F-BAR domains. Our findings reveal previously unappreciated determinants of F-BAR domain lipid-binding specificity and provide a basis for its prediction from sequence.

PubMed: 25620000
DOI: 10.1016/j.str.2014.12.009

実験手法

X-RAY DIFFRACTION (2.7 Å)