Three-dimensional structure of AAA ATPase Vps4: Advancing structural insights into the mechanisms of endosomal sorting and enveloped virus budding

Landsberg, Michael J., Vajjhala, Parimala Rao, Rothnagel, Rosalba, Munn, Alan Leslie and Hankamer, Ben (2009) Three-dimensional structure of AAA ATPase Vps4: Advancing structural insights into the mechanisms of endosomal sorting and enveloped virus budding. Structure, 17 3: 427-437. doi:10.1016/j.str.2008.12.020


Author Landsberg, Michael J.
Vajjhala, Parimala Rao
Rothnagel, Rosalba
Munn, Alan Leslie
Hankamer, Ben
Title Three-dimensional structure of AAA ATPase Vps4: Advancing structural insights into the mechanisms of endosomal sorting and enveloped virus budding
Journal name Structure   Check publisher's open access policy
ISSN 0969-2126
Publication date 2009-03-10
Year available 2009
Sub-type Article (original research)
DOI 10.1016/j.str.2008.12.020
Open Access Status DOI
Volume 17
Issue 3
Start page 427
End page 437
Total pages 10
Place of publication Cambridge, UK
Publisher Cell Press
Language eng
Subject C1
060112 Structural Biology (incl. Macromolecular Modelling)
920109 Infectious Diseases
0601 Biochemistry and Cell Biology
Abstract Vps4 is a AAA ATPase that mediates endosomal membrane protein sorting. It is also a host factor hijacked by a diverse set of clinically important viruses, including HIV and Ebola, to facilitate viral budding. Here we present the three-dimensional structure of the hydrolysis-defective Vps4pE233Q mutant. Single-particle analysis, multiangle laser light scattering, and the docking of independently determined atomic models of Vps4 monomers reveal a complex with C6 point symmetry, distinguishing between a range of previously suggested oligomeric states (8–14 subunits). The 3D reconstruction also reveals a tail-to-tail subunit organization between the two rings of the complex and identifies the location of domains critical to complex assembly and interaction with partner proteins. Our refined Vps4 structure is better supported by independent lines of evidence than those previously proposed, and provides insights into the mechanism of endosomal membrane protein sorting and viral envelope budding.
Keyword Proteins
Cellbio
Vps4
ATPase
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID 252750
DP0452362
Institutional Status UQ

 
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Created: Fri, 17 Apr 2009, 00:05:23 EST by Cody Mudgway on behalf of Institute for Molecular Bioscience