2nps: Difference between revisions

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==Overview==
==Overview==
SNARE proteins mediate membrane fusion in eukaryotic cells. They contain, conserved SNARE motifs that are usually located adjacent to a C-terminal, transmembrane domain. SNARE motifs spontaneously assemble into four helix, bundles, with each helix belonging to a different subfamily. Liposomes, containing SNAREs spontaneously fuse with each other, but it is debated, how the SNAREs are distributed between the membranes. Here, we report that, the SNAREs mediating homotypic fusion of early endosomes fuse liposomes in, five out of seven possible combinations, in contrast to previously studied, SNAREs involved in heterotypic fusion events. The crystal structure of the, early endosomal SNARE complex resembles that of the neuronal and late, endosomal complexes, but differs in surface side-chain interactions. We, conclude that homotypic fusion reactions may proceed with multiple SNARE, topologies, suggesting that the conserved SNARE structure allows for, flexibility in the initial interactions needed for fusion.
SNARE proteins mediate membrane fusion in eukaryotic cells. They contain conserved SNARE motifs that are usually located adjacent to a C-terminal transmembrane domain. SNARE motifs spontaneously assemble into four helix bundles, with each helix belonging to a different subfamily. Liposomes containing SNAREs spontaneously fuse with each other, but it is debated how the SNAREs are distributed between the membranes. Here, we report that the SNAREs mediating homotypic fusion of early endosomes fuse liposomes in five out of seven possible combinations, in contrast to previously studied SNAREs involved in heterotypic fusion events. The crystal structure of the early endosomal SNARE complex resembles that of the neuronal and late endosomal complexes, but differs in surface side-chain interactions. We conclude that homotypic fusion reactions may proceed with multiple SNARE topologies, suggesting that the conserved SNARE structure allows for flexibility in the initial interactions needed for fusion.


==About this Structure==
==About this Structure==
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[[Category: Fasshauer, D.]]
[[Category: Fasshauer, D.]]
[[Category: Jahn, R.]]
[[Category: Jahn, R.]]
[[Category: Pohl, W.H.]]
[[Category: Pohl, W H.]]
[[Category: Wahl, M.C.]]
[[Category: Wahl, M C.]]
[[Category: Walla, P.J.]]
[[Category: Walla, P J.]]
[[Category: Zwilling, D.]]
[[Category: Zwilling, D.]]
[[Category: early endosomal snare complex]]
[[Category: early endosomal snare complex]]
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[[Category: vti1a]]
[[Category: vti1a]]


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Revision as of 19:09, 21 February 2008

File:2nps.jpg


2nps, resolution 2.5Å

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Crystal Structure of the Early Endosomal SNARE Complex

OverviewOverview

SNARE proteins mediate membrane fusion in eukaryotic cells. They contain conserved SNARE motifs that are usually located adjacent to a C-terminal transmembrane domain. SNARE motifs spontaneously assemble into four helix bundles, with each helix belonging to a different subfamily. Liposomes containing SNAREs spontaneously fuse with each other, but it is debated how the SNAREs are distributed between the membranes. Here, we report that the SNAREs mediating homotypic fusion of early endosomes fuse liposomes in five out of seven possible combinations, in contrast to previously studied SNAREs involved in heterotypic fusion events. The crystal structure of the early endosomal SNARE complex resembles that of the neuronal and late endosomal complexes, but differs in surface side-chain interactions. We conclude that homotypic fusion reactions may proceed with multiple SNARE topologies, suggesting that the conserved SNARE structure allows for flexibility in the initial interactions needed for fusion.

About this StructureAbout this Structure

2NPS is a Protein complex structure of sequences from Homo sapiens, Mus musculus and Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies., Zwilling D, Cypionka A, Pohl WH, Fasshauer D, Walla PJ, Wahl MC, Jahn R, EMBO J. 2007 Jan 10;26(1):9-18. Epub 2006 Dec 7. PMID:17159904

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