1ifq: Difference between revisions

Revision as of 14:11, 21 February 2008

Sec22b N-terminal domain

OverviewOverview

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 StructureAbout this Structure

1IFQ is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Feb 21 13:11:30 2008

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OCA

@@ Line 1: / Line 1: @@
-[[Image:1ifq.jpg|left|200px]]<br /><applet load="1ifq" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ifq.jpg|left|200px]]<br /><applet load="1ifq" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ifq, resolution 2.40&Aring;" />
 '''Sec22b N-terminal domain'''<br />
 ==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.
+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==
-IFQ 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IFQ OCA].
+IFQ 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==
@@ Line 13: / Line 13: @@
 [[Category: Mus musculus]]
 [[Category: Single protein]]
-[[Category: Jr., L.C.Gonzalez.]]
+[[Category: Jr., L C.Gonzalez.]]
-[[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: five-stranded anti-parallel beta sheet]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:22:18 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:30 2008''