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Title: The Structure of the Exocyst Subunit Sec6p Defines a Conserved Architecture with Diverse Roles

Abstract

The exocyst is a conserved protein complex essential for trafficking secretory vesicles to the plasma membrane. The structure of the C-terminal domain of the exocyst subunit Sec6p reveals multiple helical bundles, which are structurally and topologically similar to Exo70p and the C-terminal domains of Exo84p and Sec15, despite <10% sequence identity. The helical bundles appear to be evolutionarily related molecular scaffolds that have diverged to create functionally distinct exocyst proteins.

Authors:
; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
914356
Report Number(s):
BNL-78924-2007-JA
TRN: US200809%%198
DOE Contract Number:
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Nat. Struct. Mol. Biol.; Journal Volume: 13; Journal Issue: 6
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; PLASMA; PROTEINS; PROTEIN STRUCTURE; national synchrotron light source

Citation Formats

Mylavarapu,S., Furgason, M., Brewer, D., and Munson, M. The Structure of the Exocyst Subunit Sec6p Defines a Conserved Architecture with Diverse Roles. United States: N. p., 2006. Web.
Mylavarapu,S., Furgason, M., Brewer, D., & Munson, M. The Structure of the Exocyst Subunit Sec6p Defines a Conserved Architecture with Diverse Roles. United States.
Mylavarapu,S., Furgason, M., Brewer, D., and Munson, M. Sun . "The Structure of the Exocyst Subunit Sec6p Defines a Conserved Architecture with Diverse Roles". United States. doi:.
@article{osti_914356,
title = {The Structure of the Exocyst Subunit Sec6p Defines a Conserved Architecture with Diverse Roles},
author = {Mylavarapu,S. and Furgason, M. and Brewer, D. and Munson, M.},
abstractNote = {The exocyst is a conserved protein complex essential for trafficking secretory vesicles to the plasma membrane. The structure of the C-terminal domain of the exocyst subunit Sec6p reveals multiple helical bundles, which are structurally and topologically similar to Exo70p and the C-terminal domains of Exo84p and Sec15, despite <10% sequence identity. The helical bundles appear to be evolutionarily related molecular scaffolds that have diverged to create functionally distinct exocyst proteins.},
doi = {},
journal = {Nat. Struct. Mol. Biol.},
number = 6,
volume = 13,
place = {United States},
year = {Sun Jan 01 00:00:00 EST 2006},
month = {Sun Jan 01 00:00:00 EST 2006}
}