1ifq
From Proteopedia
(New page: 200px<br /><applet load="1ifq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ifq, resolution 2.40Å" /> '''Sec22b N-terminal do...) |
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| - | [[Image:1ifq.jpg|left|200px]]<br /><applet load="1ifq" size=" | + | [[Image:1ifq.jpg|left|200px]]<br /><applet load="1ifq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ifq, resolution 2.40Å" /> | caption="1ifq, resolution 2.40Å" /> | ||
'''Sec22b N-terminal domain'''<br /> | '''Sec22b N-terminal domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Intra-cellular membrane fusion is facilitated by the association of SNAREs | + | 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== | ==About this Structure== | ||
| - | 1IFQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1IFQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IFQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Jr., L | + | [[Category: Jr., L C.Gonzalez.]] |
| - | [[Category: Scheller, R | + | [[Category: Scheller, R H.]] |
| - | [[Category: Weis, W | + | [[Category: Weis, W I.]] |
[[Category: GOL]] | [[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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:30 2008'' |
Revision as of 11:11, 21 February 2008
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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 with as ligand. 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
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