3b5n

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(New page: 200px<br /><applet load="3b5n" size="350" color="white" frame="true" align="right" spinBox="true" caption="3b5n, resolution 1.600&Aring;" /> '''Structure of the ye...)
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==Overview==
==Overview==
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SNARE proteins form a complex that leads to membrane fusion between, vesicles, organelles, and plasma membrane in all eukaryotic cells. We, report the 1.7 A resolution structure of the SNARE complex that mediates, exocytosis at the plasma membrane in the yeast S. cerevisiae. Similar to, its neuronal and endosomal homologues, the S. cerevisiae SNARE complex, forms a parallel four helix bundle in the center of which is an ionic, layer. The S. cerevisiae SNARE complex exhibits increased helix bending, near the ionic layer, contains water filled cavities in the complex core, and exhibits reduced thermal stability relative to mammalian SNARE, complexes. Mutagenesis experiments suggest that the water-filled cavities, contribute to the lower stability of the S. cerevisiae complex.
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SNARE proteins form a complex that leads to membrane fusion between vesicles, organelles, and plasma membrane in all eukaryotic cells. We report the 1.7A resolution structure of the SNARE complex that mediates exocytosis at the plasma membrane in the yeast Saccharomyces cerevisiae. Similar to its neuronal and endosomal homologues, the S. cerevisiae SNARE complex forms a parallel four-helix bundle in the center of which is an ionic layer. The S. cerevisiae SNARE complex exhibits increased helix bending near the ionic layer, contains water-filled cavities in the complex core, and exhibits reduced thermal stability relative to mammalian SNARE complexes. Mutagenesis experiments suggest that the water-filled cavities contribute to the lower stability of the S. cerevisiae complex.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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The structure of the yeast plasma membrane SNARE complex reveals destabilizing water filled cavities., Strop P, Kaiser SE, Vrljic M, Brunger AT, J Biol Chem. 2007 Oct 22;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17956869 17956869]
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The structure of the yeast plasma membrane SNARE complex reveals destabilizing water-filled cavities., Strop P, Kaiser SE, Vrljic M, Brunger AT, J Biol Chem. 2008 Jan 11;283(2):1113-9. Epub 2007 Oct 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17956869 17956869]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Brunger, A.T.]]
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[[Category: Brunger, A T.]]
[[Category: Strop, P.]]
[[Category: Strop, P.]]
[[Category: coiled coil]]
[[Category: coiled coil]]
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[[Category: ubl conjugation]]
[[Category: ubl conjugation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:47:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:03:31 2008''

Revision as of 17:03, 21 February 2008


3b5n, resolution 1.600Å

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Structure of the yeast plasma membrane SNARE complex

Overview

SNARE proteins form a complex that leads to membrane fusion between vesicles, organelles, and plasma membrane in all eukaryotic cells. We report the 1.7A resolution structure of the SNARE complex that mediates exocytosis at the plasma membrane in the yeast Saccharomyces cerevisiae. Similar to its neuronal and endosomal homologues, the S. cerevisiae SNARE complex forms a parallel four-helix bundle in the center of which is an ionic layer. The S. cerevisiae SNARE complex exhibits increased helix bending near the ionic layer, contains water-filled cavities in the complex core, and exhibits reduced thermal stability relative to mammalian SNARE complexes. Mutagenesis experiments suggest that the water-filled cavities contribute to the lower stability of the S. cerevisiae complex.

About this Structure

3B5N is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The structure of the yeast plasma membrane SNARE complex reveals destabilizing water-filled cavities., Strop P, Kaiser SE, Vrljic M, Brunger AT, J Biol Chem. 2008 Jan 11;283(2):1113-9. Epub 2007 Oct 22. PMID:17956869

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