This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5uj7

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 16:43, 20 November 2019

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

Structural highlights

5uj7 is a 6 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	5uj8
Gene:	ORC1, ORC1L, PARC1 (HUMAN), ORC4, ORC4L (HUMAN), ORC5, ORC5L (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[ORC1_HUMAN] Ear-patella-short stature syndrome. The disease is caused by mutations affecting the gene represented in this entry. [ORC4_HUMAN] Ear-patella-short stature syndrome. The disease is caused by mutations affecting the gene represented in this entry.

Function

[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. [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. [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]

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^[2]

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
↑ 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

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5uj7"

@@ Line 1: / Line 1: @@
 ==Structure of the active form of human Origin Recognition Complex ATPase motor module, complex subunitS 1, 4, 5==
-<StructureSection load='5uj7' size='340' side='right' caption='[[5uj7]], [[Resolution|resolution]] 3.39&Aring;' scene=''>
+<StructureSection load='5uj7' size='340' side='right'caption='[[5uj7]], [[Resolution|resolution]] 3.39&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5uj7]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UJ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UJ7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5uj7]] is a 6 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=5UJ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UJ7 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uj8|5uj8]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORC1, ORC1L, PARC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ORC4, ORC4L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ORC5, ORC5L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5uj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uj7 OCA], [http://pdbe.org/5uj7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uj7 RCSB], [http://www.ebi.ac.uk/pdbsum/5uj7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uj7 ProSAT]</span></td></tr>
 </table>
@@ Line 25: / Line 26: @@
 __TOC__
 </StructureSection>
+[[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Elkayam, E]]
 [[Category: Joshua-Tor, L]]

5uj7

From Proteopedia

Revision as of 16:43, 20 November 2019

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

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox