PDBsum entry 5fm7

Atp binding protein

PDB id: 5fm7

Contents

Protein chains

418 a.a.

422 a.a.

Ligands

ADP ×2

PDB id:

5fm7

Name:

Atp binding protein

Title:

Double-heterohexameric rings of full-length rvb1(adp)rvb2(adp)

Structure:

Rvb1. Chain: a. Engineered: yes. Rvb2. Chain: b. Engineered: yes

Source:

Chaetomium thermophilum. Organism_taxid: 209285. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: gold. Expression_system_variant: gold

Resolution:

2.90Å R-factor: 0.260 R-free: 0.282

Authors:

N.Silva-Martin,M.I.Dauden,S.Glatt,N.A.Hoffmann,C.W.Mueller

Key ref:

N.Silva-Martin et al. (2016). The Combination of X-Ray Crystallography and Cryo-Electron Microscopy Provides Insight into the Overall Architecture of the Dodecameric Rvb1/Rvb2 Complex. Plos One, 11, e0146457. PubMed id: 26745716 DOI: 10.1371/journal.pone.0146457

Date:

02-Nov-15 Release date: 20-Jan-16

Protein chain

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

Seq: 462 a.a.

Struc: 418 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: 422 a.a.

Enzyme reactions

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

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

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

reference

DOI no: 10.1371/journal.pone.0146457

Plos One 11:e0146457 (2016)

PubMed id: 26745716

The Combination of X-Ray Crystallography and Cryo-Electron Microscopy Provides Insight into the Overall Architecture of the Dodecameric Rvb1/Rvb2 Complex.

N.Silva-Martin, M.I.Daudén, S.Glatt, N.A.Hoffmann, P.Kastritis, P.Bork, M.Beck, C.W.Müller.

ABSTRACT

The Rvb1/Rvb2 complex is an essential component of many cellular pathways. The Rvb1/Rvb2 complex forms a dodecameric assembly where six copies of each subunit form two heterohexameric rings. However, due to conformational variability, the way the two rings pack together is still not fully understood. Here, we present the crystal structure and two cryo-electron microscopy reconstructions of the dodecameric, full-length Rvb1/Rvb2 complex, all showing that the interaction between the two heterohexameric rings is mediated through the Rvb1/Rvb2-specific domain II. Two conformations of the Rvb1/Rvb2 dodecamer are present in solution: a stretched conformation also present in the crystal, and a compact conformation. Novel asymmetric features observed in the reconstruction of the compact conformation provide additional insight into the plasticity of the Rvb1/Rvb2 complex.