4OIY

Crystal structure of Sec7p catalytic domain

4OIY の概要

• エントリーDOI: 10.2210/pdb4oiy/pdb
• 分子名称: Protein transport protein SEC7, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: sec7 domain, guanine nucleotide exchange protein for arf, protein transport
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Cytoplasm: P11075
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42843.19

構造登録者

Qiu, B.,Zhang, K.,Sun, F. (登録日: 2014-01-20, 公開日: 2014-07-02, 最終更新日: 2023-11-08)

主引用文献

Qiu, B.,Zhang, K.,Wang, S.L.,Sun, F.
C-terminal motif within Sec7 domain regulates guanine nucleotide exchange activity via tuning protein conformation
Biochem.Biophys.Res.Commun., 446:380-386, 2014

PubMed Abstract: ADP-ribosylation factors (Arfs) play key roles in controlling membrane traffic and organelle structures. The activation of Arfs from GDP to GTP binding form is triggered by the guanine exchange factors (GEFs). There are six families of Arf-GEFs with a common guanine exchange catalytic domain (Sec7 domain) and various mechanisms of guanine exchange activity regulation. A loop region (loop>J motif) just following the helix J of Sec7 domain was found conserved and important for the catalytic activity regulation of Arf-GEFs. However, the molecular detail of the role the loop>J motif plays has been yet unclear. Here, we studied the catalytic domain of Sec7p, a yeast trans-Golgi network membrane localized Arf-GEFs, and found that the loop>J motif is indispensible for its GEF catalytic activity. Crystallographic, NMR spectrum and mutagenesis studies suggested that the loop>J motif with a key conserved residue Ile1010 modulates the fine conformation of Sec7 domain and thereby regulates its guanine exchange activity.

PubMed: 24613384
DOI: 10.1016/j.bbrc.2014.02.125

実験手法

X-RAY DIFFRACTION (1.5 Å)