4OIY

Crystal structure of Sec7p catalytic domain

Summary for 4OIY

• Entry DOI: 10.2210/pdb4oiy/pdb
• Descriptor: Protein transport protein SEC7, MAGNESIUM ION (3 entities in total)
• Functional Keywords: sec7 domain, guanine nucleotide exchange protein for arf, protein transport
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Cytoplasm: P11075
• Total number of polymer chains: 2
• Total formula weight: 42843.19

Authors

Qiu, B.,Zhang, K.,Sun, F. (deposition date: 2014-01-20, release date: 2014-07-02, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.5 Å)