4LGM

Crystal Structure of Sulfolobus solfataricus Vps4

4LGM の概要

• エントリーDOI: 10.2210/pdb4lgm/pdb
• 分子名称: Vps4 AAA ATPase, CHLORIDE ION (3 entities in total)
• 機能のキーワード: atp hydrolysis, hydrolase
• 由来する生物種: Sulfolobus solfataricus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33605.25

構造登録者

Han, H.,Hill, C.P.,Whitby, F.G.,Monroe, N. (登録日: 2013-06-28, 公開日: 2013-11-06, 最終更新日: 2024-02-28)

主引用文献

Monroe, N.,Han, H.,Gonciarz, M.D.,Eckert, D.M.,Karren, M.A.,Whitby, F.G.,Sundquist, W.I.,Hill, C.P.
The Oligomeric State of the Active Vps4 AAA ATPase.
J.Mol.Biol., 426:510-525, 2014

PubMed Abstract: The cellular ESCRT (endosomal sorting complexes required for transport) pathway drives membrane constriction toward the cytosol and effects membrane fission during cytokinesis, endosomal sorting, and the release of many enveloped viruses, including the human immunodeficiency virus. A component of this pathway, the AAA ATPase Vps4, provides energy for pathway progression. Although it is established that Vps4 functions as an oligomer, subunit stoichiometry and other fundamental features of the functional enzyme are unclear. Here, we report that although some mutant Vps4 proteins form dodecameric assemblies, active wild-type Saccharomyces cerevisiae and Sulfolobus solfataricus Vps4 enzymes can form hexamers in the presence of ATP and ADP, as assayed by size-exclusion chromatography and equilibrium analytical ultracentrifugation. The Vta1p activator binds hexameric yeast Vps4p without changing the oligomeric state of Vps4p, implying that the active Vta1p-Vps4p complex also contains a single hexameric ring. Additionally, we report crystal structures of two different archaeal Vps4 homologs, whose structures and lattice interactions suggest a conserved mode of oligomerization. Disruption of the proposed hexamerization interface by mutagenesis abolished the ATPase activity of archaeal Vps4 proteins and blocked Vps4p function in S. cerevisiae. These data challenge the prevailing model that active Vps4 is a double-ring dodecamer, and argue that, like other type I AAA ATPases, Vps4 functions as a single ring with six subunits.

PubMed: 24161953
DOI: 10.1016/j.jmb.2013.09.043

実験手法

X-RAY DIFFRACTION (2.711 Å)