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5UJ8

Human Origin Recognition Complex subunits 2 and 3

Summary for 5UJ8
Entry DOI10.2210/pdb5uj8/pdb
Related5uj7
DescriptorOrigin recognition complex subunit 3, Origin recognition complex subunit 2 (2 entities in total)
Functional Keywordsorc, replication, atpase, hydrolase
Biological sourceHomo sapiens (Human)
More
Cellular locationNucleus: Q9UBD5 Q13416
Total number of polymer chains8
Total formula weight490983.64
Authors
Tocilj, A.,On, K.F.,Elkayam, E.,Joshua-Tor, L. (deposition date: 2017-01-17, release date: 2017-02-08, Last modification date: 2024-10-23)
Primary citationTocilj, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (6 Å)
Structure validation

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