5UJ7

Structure of the active form of human Origin Recognition Complex ATPase motor module, complex subunitS 1, 4, 5

Summary for 5UJ7

• Entry DOI: 10.2210/pdb5uj7/pdb
• Related: 5uj8
• Descriptor: Origin recognition complex subunit 1, Origin recognition complex subunit 4, Origin recognition complex subunit 5, ... (6 entities in total)
• Functional Keywords: replication, dna-binding, aaa+ atpase, dna binding protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 6
• Total formula weight: 258738.49

Authors

Tocilj, A.,Elkayam, E.,On, K.F.,Joshua-Tor, L. (deposition date: 2017-01-17, release date: 2017-02-08, Last modification date: 2023-10-04)

Primary citation

Tocilj, A.,On, K.F.,Yuan, Z.,Sun, J.,Elkayam, E.,Li, H.,Stillman, B.,Joshua-Tor, L.
Structure of the active form of human Origin Recognition Complex and its ATPase motor module.
Elife, 6:-, 2017

PubMed Abstract: Binding of the Origin Recognition Complex (ORC) to origins of replication marks the first step in the initiation of replication of the genome in all eukaryotic cells. Here, we report the structure of the active form of human ORC determined by X-ray crystallography and cryo-electron microscopy. The complex is composed of an ORC1/4/5 motor module lobe in an organization reminiscent of the DNA polymerase clamp loader complexes. A second lobe contains the ORC2/3 subunits. The complex is organized as a double-layered shallow corkscrew, with the AAA+ and AAA+-like domains forming one layer, and the winged-helix domains (WHDs) forming a top layer. CDC6 fits easily between ORC1 and ORC2, completing the ring and the DNA-binding channel, forming an additional ATP hydrolysis site. Analysis of the ATPase activity of the complex provides a basis for understanding ORC activity as well as molecular defects observed in Meier-Gorlin Syndrome mutations.

PubMed: 28112645
DOI: 10.7554/eLife.20818

Experimental method

X-RAY DIFFRACTION (3.394 Å)