1EPU

X-RAY crystal structure of neuronal SEC1 from squid

Summary for 1EPU

Entry DOI	10.2210/pdb1epu/pdb
Related	1DN1
Descriptor	S-SEC1 (2 entities in total)
Functional Keywords	parallel beta-sheets, left-hand turn connection, helical bundle, endocytosis-exocytosis complex, endocytosis/exocytosis
Biological source	Loligo pealei
Total number of polymer chains	1
Total formula weight	68815.47
Authors	Bracher, A.,Perrakis, A.,Dresbach, T.,Betz, H.,Weissenhorn, W. (deposition date: 2000-03-29, release date: 2000-08-09, Last modification date: 2024-10-30)
Primary citation	Bracher, A.,Perrakis, A.,Dresbach, T.,Betz, H.,Weissenhorn, W. The X-ray crystal structure of neuronal Sec1 from squid sheds new light on the role of this protein in exocytosis. Structure Fold.Des., 8:685-694, 2000 Cited by PubMed Abstract: Sec1-like molecules have been implicated in a variety of eukaryotic vesicle transport processes including neurotransmitter release by exocytosis. They regulate vesicle transport by binding to a t-SNARE from the syntaxin family. This process is thought to prevent SNARE complex formation, a protein complex required for membrane fusion. Whereas Sec1 molecules are essential for neurotransmitter release and other secretory events, their interaction with syntaxin molecules seems to represent a negative regulatory step in secretion. PubMed: 10903948 DOI: 10.1016/S0969-2126(00)00156-8 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.4 Å)

Structure validation