PDBsum entry 4lcb

Protein transport

PDB id: 4lcb

Contents

Protein chain

252 a.a.

Metals

_CL

Waters ×101

PDB id:

4lcb

Name:

Protein transport

Title:

Structure of vps4 homolog from acidianus hospitalis

Structure:

Cell division protein cdvc, vps4. Chain: a. Engineered: yes

Source:

Acidianus hospitalis. Organism_taxid: 933801. Strain: w1. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.08Å R-factor: 0.216 R-free: 0.254

Authors:

H.Han,C.P.Hill,F.G.Whitby,N.Monroe

Key ref:

N.Monroe et al. (2014). The oligomeric state of the active Vps4 AAA ATPase. J Mol Biol, 426, 510-525. PubMed id: 24161953 DOI: 10.1016/j.jmb.2013.09.043

Date:

21-Jun-13 Release date: 06-Nov-13

Protein chain

F4B4B0  (F4B4B0_ACIHW) -  Cell division protein CdvC, Vps4 from Acidianus hospitalis (strain W1)

Seq: 365 a.a.

Struc: 252 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.jmb.2013.09.043

J Mol Biol 426:510-525 (2014)

PubMed id: 24161953

The oligomeric state of the active Vps4 AAA ATPase.

N.Monroe, H.Han, M.D.Gonciarz, D.M.Eckert, M.A.Karren, F.G.Whitby, W.I.Sundquist, C.P.Hill.

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.