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1ifq
From Proteopedia
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|PDB= 1ifq |SIZE=350|CAPTION= <scene name='initialview01'>1ifq</scene>, resolution 2.40Å | |PDB= 1ifq |SIZE=350|CAPTION= <scene name='initialview01'>1ifq</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ifq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ifq OCA], [http://www.ebi.ac.uk/pdbsum/1ifq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ifq RCSB]</span> | ||
}} | }} | ||
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[[Category: Scheller, R H.]] | [[Category: Scheller, R H.]] | ||
[[Category: Weis, W I.]] | [[Category: Weis, W I.]] | ||
| - | [[Category: GOL]] | ||
[[Category: alpha/beta 3-layer sandwich]] | [[Category: alpha/beta 3-layer sandwich]] | ||
[[Category: five-stranded anti-parallel beta sheet]] | [[Category: five-stranded anti-parallel beta sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:19:10 2008'' |
Revision as of 18:19, 30 March 2008
| |||||||
| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Sec22b N-terminal domain
Overview
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.
About this Structure
1IFQ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
A novel snare N-terminal domain revealed by the crystal structure of Sec22b., Gonzalez LC Jr, Weis WI, Scheller RH, J Biol Chem. 2001 Jun 29;276(26):24203-11. Epub 2001 Apr 17. PMID:11309394
Page seeded by OCA on Sun Mar 30 21:19:10 2008
