MukBEF(E1407Q)-MatP-DNA in the presence of ATP
Ontology highlight
ABSTRACT:
SUBMITTER: Frank Bürmann
PROVIDER: EMPIAR-10755 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Cryo-EM structure of MukBEF reveals DNA loop entrapment at chromosomal unloading sites.
Bürmann Frank F Funke Louise F H LFH Chin Jason W JW Löwe Jan J
Molecular cell 20211104 23
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 correspo ...[more]
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