1IFQ

Sec22b N-terminal domain

1IFQ の概要

• エントリーDOI: 10.2210/pdb1ifq/pdb
• 分子名称: vesicle trafficking protein Sec22b, GLYCEROL (3 entities in total)
• 機能のキーワード: five-stranded anti-parallel beta sheet, alpha/beta 3-layer sandwich, protein transport
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type IV membrane protein (By similarity): O08547
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32223.79

構造登録者

Gonzalez Jr., L.C.,Weis, W.I.,Scheller, R.H. (登録日: 2001-04-13, 公開日: 2001-05-02, 最終更新日: 2024-11-20)

主引用文献

Gonzalez Jr., L.C.,Weis, W.I.,Scheller, R.H.
A novel snare N-terminal domain revealed by the crystal structure of Sec22b.
J.Biol.Chem., 276:24203-24211, 2001

PubMed Abstract: Intra-cellular membrane fusion is facilitated by the association of SNAREs from opposite membranes into stable alpha-helical bundles. Many SNAREs, in addition to their alpha-helical regions, contain N-terminal domains that likely have essential regulatory functions. To better understand this regulation, we have determined the 2.4-A crystal structure of the 130-amino acid N-terminal domain of mouse Sec22b (mSec22b), a SNARE involved in endoplasmic reticulum/Golgi membrane trafficking. The domain consists of a mixed alpha-helical/beta-sheet fold that resembles a circular permutation of the actin/poly-proline binding protein, profilin, and the GAF/PAS family of regulatory modules. The structure is distinct from the previously characterized N-terminal domain of syntaxin 1A, and, unlike syntaxin 1A, the N-terminal domain of mSec22b has no effect on the rate of SNARE assembly in vitro. An analysis of surface conserved residues reveals a potential protein interaction site. Key residues in this site are distinct in two mammalian Sec22 variants that lack SNARE domains. Finally, sequence analysis indicates that a similar domain is likely present in the endosomal/lysosomal SNARE VAMP7.

PubMed: 11309394
DOI: 10.1074/jbc.M101584200

実験手法

X-RAY DIFFRACTION (2.4 Å)