4FBK
Crystal structure of a covalently fused Nbs1-Mre11 complex with one manganese ion per active site
Summary for 4FBK
| Entry DOI | 10.2210/pdb4fbk/pdb |
| Related | 4FBQ 4FBW 4FCX |
| Descriptor | DNA repair and telomere maintenance protein nbs1,DNA repair protein rad32 CHIMERIC PROTEIN, SULFATE ION, MANGANESE (II) ION, ... (4 entities in total) |
| Functional Keywords | dna double-strand break repair, nuclease, schizosaccharomyces pombe, hydrolase, protein binding |
| Biological source | Schizosaccharomyces pombe More |
| Cellular location | Nucleus : Q09683 |
| Total number of polymer chains | 2 |
| Total formula weight | 107197.96 |
| Authors | Schiller, C.B.,Lammens, K.,Hopfner, K.P. (deposition date: 2012-05-23, release date: 2012-06-20, Last modification date: 2024-02-28) |
| Primary citation | Schiller, C.B.,Lammens, K.,Guerini, I.,Coordes, B.,Feldmann, H.,Schlauderer, F.,Mockel, C.,Schele, A.,Strasser, K.,Jackson, S.P.,Hopfner, K.P. Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. Nat.Struct.Mol.Biol., 19:693-700, 2012 Cited by PubMed Abstract: The Mre11-Rad50-Nbs1 (MRN) complex tethers, processes and signals DNA double-strand breaks, promoting genomic stability. To understand the functional architecture of MRN, we determined the crystal structures of the Schizosaccharomyces pombe Mre11 dimeric catalytic domain alone and in complex with a fragment of Nbs1. Two Nbs1 subunits stretch around the outside of the nuclease domains of Mre11, with one subunit additionally bridging and locking the Mre11 dimer via a highly conserved asymmetrical binding motif. Our results show that Mre11 forms a flexible dimer and suggest that Nbs1 not only is a checkpoint adaptor but also functionally influences Mre11-Rad50. Clinical mutations in Mre11 are located along the Nbs1-interaction sites and weaken the Mre11-Nbs1 interaction. However, they differentially affect DNA repair and telomere maintenance in Saccharomyces cerevisiae, potentially providing insight into their different human disease pathologies. PubMed: 22705791DOI: 10.1038/nsmb.2323 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.379 Å) |
Structure validation
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