PDBsum entry 4wvy

Hydrolase

PDB id: 4wvy

Contents

Protein chains

427 a.a.

408 a.a.

Ligands

ATP

PDB id:

4wvy

Name:

Hydrolase

Title:

Double-heterohexameric rings of full-length rvb1(atp)/rvb2(apo)

Structure:

Ruvb-like 1. Chain: a. Engineered: yes. Ruvb-like 2. Chain: b. Engineered: yes

Source:

Chaetomium thermophilum. Organism_taxid: 759272. Strain: dsm 1495 / cbs 144.50 / imi 039719. Gene: ctht_0006820. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: rosetta 2. Gene: ctht_0006170.

Resolution:

3.64Å R-factor: 0.223 R-free: 0.251

Authors:

K.-P.Hopfner,K.Lakomek

Key ref:

K.Lakomek et al. (2015). Structural basis for dodecameric assembly states and conformational plasticity of the full-length AAA+ ATPases Rvb1 · Rvb2. Structure, 23, 483-495. PubMed id: 25661652 DOI: 10.1016/j.str.2014.12.015

Date:

08-Nov-14 Release date: 18-Feb-15

Protein chain

G0RYI5  (G0RYI5_CHATD) -  RuvB-like helicase from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

Seq: 462 a.a.

Struc: 427 a.a.

Protein chain

G0RYC2  (G0RYC2_CHATD) -  RuvB-like helicase from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

Seq: 488 a.a.

Struc: 408 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.3.6.4.12 - Dna helicase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

ATP (Bound ligand (Het Group name = ATP) corresponds exactly) + H2O = ADP + phosphate + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.str.2014.12.015

Structure 23:483-495 (2015)

PubMed id: 25661652

Structural basis for dodecameric assembly states and conformational plasticity of the full-length AAA+ ATPases Rvb1 · Rvb2.

K.Lakomek, G.Stoehr, A.Tosi, M.Schmailzl, K.P.Hopfner.

ABSTRACT

As building blocks of diverse macromolecular complexes, the AAA+ ATPases Rvb1 and Rvb2 are crucial for many cellular activities including cancer-related processes. Their oligomeric structure and function remain unclear. We report the crystal structures of full-length heteromeric Rvb1·Rvb2 complexes in distinct nucleotide binding states. Chaetomium thermophilum Rvb1·Rvb2 assemble into hexameric rings of alternating molecules and into stable dodecamers. Intriguingly, the characteristic oligonucleotide-binding (OB) fold domains (DIIs) of Rvb1 and Rvb2 occupy unequal places relative to the compact AAA+ core ring. While Rvb1's DII forms contacts between hexamers, Rvb2's DII is rotated 100° outward, occupying lateral positions. ATP was retained bound to Rvb1 but not Rvb2 throughout purification, suggesting nonconcerted ATPase activities and nucleotide binding. Significant conformational differences between nucleotide-free and ATP-/ADP-bound states in the crystal structures and in solution suggest that the functional role of Rvb1·Rvb2 is mediated by highly interconnected structural switches. Our structures provide an atomic framework for dodecameric states and Rvb1·Rvb2's conformational plasticity.