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1IFQ

Sec22b N-terminal domain

Summary for 1IFQ
Entry DOI10.2210/pdb1ifq/pdb
Descriptorvesicle trafficking protein Sec22b, GLYCEROL (3 entities in total)
Functional Keywordsfive-stranded anti-parallel beta sheet, alpha/beta 3-layer sandwich, protein transport
Biological sourceMus musculus (house mouse)
Cellular locationEndoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type IV membrane protein (By similarity): O08547
Total number of polymer chains2
Total formula weight32223.79
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 citationGonzalez 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: 11309394
DOI: 10.1074/jbc.M101584200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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