PDBsum entry 3av0

Recombination

PDB id: 3av0

Contents

Protein chains

369 a.a.

365 a.a.

Ligands

GOL ×4

IPA ×3

SO4

AGS

Metals

_MG

Waters ×20

PDB id:

3av0

Name:

Recombination

Title:

Crystal structure of mre11-rad50 bound to atp s

Structure:

DNA double-strand break repair protein mre11. Chain: a. Fragment: nuclease domain (unp residues 1-313). Engineered: yes. DNA double-strand break repair rad50 atpase. Chain: b. Fragment: abc atpase domain (unp residues 1-190, 825-1005). Synonym: rad50 abc-atpase. Engineered: yes.

Source:

Methanocaldococcus jannaschii. Organism_taxid: 2190. Gene: rad50, mj1322. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562

Resolution:

3.10Å R-factor: 0.221 R-free: 0.276

Authors:

H.S.Lim,J.S.Kim,Y.Cho

Key ref:

H.S.Lim et al. (2011). Crystal structure of the Mre11-Rad50-ATPγS complex: understanding the interplay between Mre11 and Rad50. Genes Dev, 25, 1091-1104. PubMed id: 21511873

Date:

18-Feb-11 Release date: 25-May-11

Protein chain

Q58719  (MRE11_METJA) -  DNA double-strand break repair protein Mre11 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

Seq: 366 a.a.

Struc: 369 a.a.

Protein chain

Q58718  (RAD50_METJA) -  DNA double-strand break repair Rad50 ATPase from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

Seq: 1005 a.a.

Struc: 365 a.a.*

* PDB and UniProt seqs differ at 142 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: Chain A: E.C.3.1.-.-
• Enzyme class 2: Chain B: E.C.?

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Genes Dev 25:1091-1104 (2011)

PubMed id: 21511873

Crystal structure of the Mre11-Rad50-ATPγS complex: understanding the interplay between Mre11 and Rad50.

H.S.Lim, J.S.Kim, Y.B.Park, G.H.Gwon, Y.Cho.

ABSTRACT

Communication between Mre11 and Rad50 in the MR complex is critical for the sensing, damage signaling, and repair of DNA double-strand breaks. To understand the basis for interregulation between Mre11 and Rad50, we determined the crystal structure of the Mre11-Rad50-ATPγS complex. Mre11 brings the two Rad50 molecules into close proximity and promotes ATPase activity by (1) holding the coiled-coil arm of Rad50 through its C-terminal domain, (2) stabilizing the signature motif and P loop of Rad50 via its capping domain, and (3) forming a dimer through the nuclease domain. ATP-bound Rad50 negatively regulates the nuclease activity of Mre11 by blocking the active site of Mre11. Hydrolysis of ATP disengages Rad50 molecules, and, concomitantly, the flexible linker that connects the C-terminal domain and the capping domain of Mre11 undergoes substantial conformational change to relocate Rad50 and unmask the active site of Mre11. Our structural and biochemical data provide insights into understanding the interplay between Mre11 and Rad50 to facilitate efficient DNA damage repair.