7NYZ
Cryo-EM structure of the MukBEF-MatP-DNA monomer (partially open conformation)
Summary for 7NYZ
| Entry DOI | 10.2210/pdb7nyz/pdb |
| EMDB information | 12659 |
| Descriptor | Chromosome partition protein MukB, ADENOSINE-5'-TRIPHOSPHATE, 4'-PHOSPHOPANTETHEINE, ... (11 entities in total) |
| Functional Keywords | smc-kleisin complex, atpase, dna binding protein |
| Biological source | Photorhabdus thracensis More |
| Total number of polymer chains | 14 |
| Total formula weight | 618624.14 |
| Authors | Buermann, F.,Lowe, J. (deposition date: 2021-03-23, release date: 2021-07-07, Last modification date: 2022-03-23) |
| Primary citation | Burmann, F.,Funke, L.F.H.,Chin, J.W.,Lowe, J. Cryo-EM structure of MukBEF reveals DNA loop entrapment at chromosomal unloading sites. Mol.Cell, 81:4891-4906.e8, 2021 Cited by PubMed Abstract: The ring-like structural maintenance of chromosomes (SMC) complex MukBEF folds the genome of Escherichia coli and related bacteria into large loops, presumably by active DNA loop extrusion. MukBEF activity within the replication terminus macrodomain is suppressed by the sequence-specific unloader MatP. Here, we present the complete atomic structure of MukBEF in complex with MatP and DNA as determined by electron cryomicroscopy (cryo-EM). The complex binds two distinct DNA double helices corresponding to the arms of a plectonemic loop. MatP-bound DNA threads through the MukBEF ring, while the second DNA is clamped by the kleisin MukF, MukE, and the MukB ATPase heads. Combinatorial cysteine cross-linking confirms this topology of DNA loop entrapment in vivo. Our findings illuminate how a class of near-ubiquitous DNA organizers with important roles in genome maintenance interacts with the bacterial chromosome. PubMed: 34739874DOI: 10.1016/j.molcel.2021.10.011 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.5 Å) |
Structure validation
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