1IFQ
Sec22b N-terminal domain
Summary for 1IFQ
| Entry DOI | 10.2210/pdb1ifq/pdb |
| Descriptor | vesicle trafficking protein Sec22b, GLYCEROL (3 entities in total) |
| Functional Keywords | five-stranded anti-parallel beta sheet, alpha/beta 3-layer sandwich, protein transport |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type IV membrane protein (By similarity): O08547 |
| Total number of polymer chains | 2 |
| Total formula weight | 32223.79 |
| Authors | Gonzalez Jr., L.C.,Weis, W.I.,Scheller, R.H. (deposition date: 2001-04-13, release date: 2001-05-02, Last modification date: 2024-11-20) |
| Primary citation | 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 Cited by 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: 11309394DOI: 10.1074/jbc.M101584200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
Download full validation report






