PDBsum entry: 1bvs

DNA binding protein

PDB id: 1bvs

Contents

Protein chains

(+ 2 more) 183 a.a. *

* Residue conservation analysis

PDB id:

1bvs

Name:

DNA binding protein

Title:

Ruva complexed to a holliday junction.

Structure:

Protein (holliday junction DNA helicase ruva). Chain: a, b, c, d, e, f, g, h. Engineered: yes

Source:

Mycobacterium leprae. Organism_taxid: 1769. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: bl21(de3).

Biol. unit:

Octamer (from PDB file)

Resolution:

3.00Å R-factor: 0.274 R-free: 0.319

Authors:

S.M.Roe,L.H.Pearl

Key ref:

S.M.Roe et al. (1998). Crystal structure of an octameric RuvA-Holliday junction complex. Mol Cell, 2, 361-372. PubMed id: 9774974 DOI: 10.1016/S1097-2765(00)80280-4

Date:

17-Sep-98 Release date: 23-Sep-98

Protein chains

P40832  (RUVA_MYCLE) -  Holliday junction ATP-dependent DNA helicase RuvA

Seq: 203 a.a.

Struc: 183 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.6.4.12 - Dna helicase.
• Reaction: ATP + H₂O = ADP + phosphate

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

 Gene Ontology (GO) functional annotation 

• Cellular component: Holliday junction helicase complex (1 term)
• Biological process: response to DNA damage stimulus (4 terms)
• Biochemical function: nucleotide binding (7 terms)

reference

DOI no: 10.1016/S1097-2765(00)80280-4

Mol Cell 2:361-372 (1998)

PubMed id: 9774974

Crystal structure of an octameric RuvA-Holliday junction complex.

S.M.Roe, T.Barlow, T.Brown, M.Oram, A.Keeley, I.R.Tsaneva, L.H.Pearl.

ABSTRACT

Holliday junctions occur as intermediates in homologous recombination and DNA repair. In bacteria, resolution of Holliday junctions is accomplished by the RuvABC system, consisting of a junction-specific helicase complex RuvAB, which promotes branch migration, and a junction-specific endonuclease RuvC, which nicks two strands. The crystal structure of a complex between the RuvA protein of M. leprae and a synthetic four-way junction has now been determined. Rather than binding on the open surface of a RuvA tetramer as previously suggested, the DNA is sandwiched between two RuvA tetramers, which form a closed octameric shell, stabilized by a conserved tetramer-tetramer interface. Interactions between the DNA backbone and helix-hairpin-helix motifs from both tetramers suggest a mechanism for strand separation promoted by RuvA.

Selected figure(s)

Figure 4.
Figure 4. Cruciform CavernSurface picture of the cruciform cavern generated by the octameric protein shell of M. leprae RuvA. The protein surface has been transected through the center of gravity of the complex, in the Up–Down/East–West plane, and is viewed from the North. The surface is colored according to the distance from the center of gravity, going from red (closest) to blue (farthest). The stalagmite–stalactite structure formed by the side chains of the eight copies of Glu-54 can clearly be seen (in red) constricting the height of the cavern at its center.

Figure 7.
Figure 7. RuvA as the Stator for the RuvB Motor(a) Schematic diagram of the proposed RuvAB branch migration complex based on [39]. In the “unstable” form with only one RuvA tetramer bound, the torque generated by the counterrotating RuvB motors would cause the RuvA tetramer to rotate around its own axis, disrupting interactions with DNA. In the “stable” form with the RuvA octamer described here, the twisting of one RuvA tetramer is opposed by the counter motion of the other tetramer, stabilizing the complex for branch migration. In a putative RuvABC resolution complex, interactions between a RuvC dimer and RuvB motors might provide sufficient stability for limited branch migration even when only one RuvA tetramer is bound.(b) Space-filling picture of the M. leprae RuvA octamer shell. The C-terminal domains (in red), which are essential for RuvB interactions, are arrayed on either side of the mouths of the tunnels.

The above figures are reprinted by permission from Cell Press: Mol Cell (1998, 2, 361-372) copyright 1998.

Figures were selected by an automated process.