1EZ3

CRYSTAL STRUCTURE OF THE NEURONAL T-SNARE SYNTAXIN-1A

1EZ3 の概要

• エントリーDOI: 10.2210/pdb1ez3/pdb
• 分子名称: SYNTAXIN-1A (2 entities in total)
• 機能のキーワード: three helix bundle, endocytosis-exocytosis complex, endocytosis/exocytosis
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein (By similarity): P32851
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44936.44

構造登録者

Lerman, J.C.,Robblee, J.,Fairman, R.,Hughson, F.M. (登録日: 2000-05-09, 公開日: 2000-06-07, 最終更新日: 2024-02-07)

主引用文献

Lerman, J.C.,Robblee, J.,Fairman, R.,Hughson, F.M.
Structural analysis of the neuronal SNARE protein syntaxin-1A.
Biochemistry, 39:8470-8479, 2000

PubMed Abstract: Intracellular trafficking depends on the docking and fusion of transport vesicles with cellular membranes. Central to docking and fusion is the pairing of SNARE proteins (soluble NSF attachment protein receptors) associated with the vesicle and target membranes (v- and t-SNAREs, respectively). Here, the X-ray structure of an N-terminal conserved domain of the neuronal t-SNARE syntaxin-1A was determined to a resolution of 1.9 A using multiwavelength anomalous diffraction. This X-ray structure, which is in general agreement with an NMR structure of a similar fragment, provides new insight into the interaction surface between the N-terminal domain and the remainder of the protein. In vitro characterization of the intact cytoplasmic domain of syntaxin revealed that it forms dimers, and probably tetramers, at low micromolar concentrations, with concomitant structural changes that can be detected by limited proteolysis. These observations suggest that the promiscuity characteristic of pairing between v-SNAREs and t-SNAREs extends to the formation of homo-oligomeric t-SNARE complexes as well. They also suggest a potential role for the neuronal Sec1 protein (nSec1) in preventing the formation of syntaxin multimers.

PubMed: 10913252
DOI: 10.1021/bi0003994

実験手法

X-RAY DIFFRACTION (1.9 Å)