1XT0

The Structure of N-terminal Sec7 domain of RalF

1XT0 の概要

• エントリーDOI: 10.2210/pdb1xt0/pdb
• 関連するPDBエントリー: 1XSZ
• 分子名称: guanine nucleotide exchange protein (2 entities in total)
• 機能のキーワード: the n-terminal sec7 domain of ralf, signaling protein
• 由来する生物種: Legionella pneumophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23076.44

構造登録者

Amor, J.C.,Swails, J.,Roy, C.R.,Nagai, H.,Ingmundson, A.,Cheng, X.,Kahn, R.A. (登録日: 2004-10-20, 公開日: 2004-11-02, 最終更新日: 2023-11-15)

主引用文献

Amor, J.C.,Swails, J.,Zhu, X.,Roy, C.R.,Nagai, H.,Ingmundson, A.,Cheng, X.,Kahn, R.A.
The structure of RalF, an ADP-ribosylation factor guanine nucleotide exchange factor from Legionella pneumophila, reveals the presence of a cap over the active site
J.Biol.Chem., 280:1392-1400, 2005

PubMed Abstract: The Legionella pneumophila protein RalF is secreted into host cytosol via the Dot/Icm type IV transporter where it acts to recruit ADP-ribosylation factor (Arf) to pathogen-containing phagosomes in the establishment of a replicative organelle. The presence in RalF of the Sec7 domain, present in all Arf guanine nucleotide exchange factors, has suggested that recruitment of Arf is an early step in pathogenesis. We have determined the crystal structure of RalF and of the isolated Sec7 domain and found that RalF is made up of two domains. The Sec7 domain is homologous to mammalian Sec7 domains. The C-terminal domain forms a cap over the active site in the Sec7 domain and contains a conserved folding motif, previously observed in adaptor subunits of vesicle coat complexes. The importance of the capping domain and of the glutamate in the "glutamic finger," conserved in all Sec7 domains, to RalF functions was examined using three different assays. These data highlight the functional importance of domains other than Sec7 in Arf guanine nucleotide exchange factors to biological activities and suggest novel mechanisms of regulation of those activities.

PubMed: 15520000
DOI: 10.1074/jbc.M410820200

実験手法

X-RAY DIFFRACTION (2.16 Å)