<table><tr><td colspan='2'>[[5ujm]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UJM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UJM FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ujm]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UJM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UJM FirstGlance]. <br>
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[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Elkayam, E]]
[[Category: Elkayam, E]]
[[Category: Joshua-Tor, L]]
[[Category: Joshua-Tor, L]]
Revision as of 19:43, 6 March 2020
Structure of the active form of human Origin Recognition Complex and its ATPase motor module
5ujm is a 5 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[ORC4_HUMAN] Ear-patella-short stature syndrome. The disease is caused by mutations affecting the gene represented in this entry. [ORC1_HUMAN] Ear-patella-short stature syndrome. The disease is caused by mutations affecting the gene represented in this entry.
Function
[ORC4_HUMAN] Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3.[1] [ORC1_HUMAN] Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. [ORC3_HUMAN] Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3.[2] [ORC2_HUMAN] Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K20me3 and H4K27me3. Stabilizes LRWD1, by protecting it from ubiquitin-mediated proteasomal degradation. Also stabilizes ORC3.[3][4] [ORC5_HUMAN] Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
Publication Abstract from PubMed
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.
Structure of the active form of human origin recognition complex and its ATPase motor module.,Tocilj A, On KF, Yuan Z, Sun J, Elkayam E, Li H, Stillman B, Joshua-Tor L Elife. 2017 Jan 23;6. pii: e20818. doi: 10.7554/eLife.20818. PMID:28112645[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Chan KM, Zhang Z. Leucine-rich repeat and WD repeat-containing protein 1 is recruited to pericentric heterochromatin by trimethylated lysine 9 of histone H3 and maintains heterochromatin silencing. J Biol Chem. 2012 Apr 27;287(18):15024-33. doi: 10.1074/jbc.M111.337980. Epub, 2012 Mar 15. PMID:22427655 doi:http://dx.doi.org/10.1074/jbc.M111.337980
↑ Chan KM, Zhang Z. Leucine-rich repeat and WD repeat-containing protein 1 is recruited to pericentric heterochromatin by trimethylated lysine 9 of histone H3 and maintains heterochromatin silencing. J Biol Chem. 2012 Apr 27;287(18):15024-33. doi: 10.1074/jbc.M111.337980. Epub, 2012 Mar 15. PMID:22427655 doi:http://dx.doi.org/10.1074/jbc.M111.337980
↑ Chan KM, Zhang Z. Leucine-rich repeat and WD repeat-containing protein 1 is recruited to pericentric heterochromatin by trimethylated lysine 9 of histone H3 and maintains heterochromatin silencing. J Biol Chem. 2012 Apr 27;287(18):15024-33. doi: 10.1074/jbc.M111.337980. Epub, 2012 Mar 15. PMID:22427655 doi:http://dx.doi.org/10.1074/jbc.M111.337980
↑ Shen Z, Prasanth SG. Orc2 protects ORCA from ubiquitin-mediated degradation. Cell Cycle. 2012 Oct 1;11(19):3578-89. doi: 10.4161/cc.21870. Epub 2012 Aug 30. PMID:22935713 doi:http://dx.doi.org/10.4161/cc.21870
↑ Tocilj A, On KF, 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. 2017 Jan 23;6. pii: e20818. doi: 10.7554/eLife.20818. PMID:28112645 doi:http://dx.doi.org/10.7554/eLife.20818
