5ujm

From Proteopedia

(Difference between revisions)

Revision as of 09:31, 10 March 2017

Structure of the active form of human Origin Recognition Complex and its ATPase motor module

Structural highlights

5ujm is a 5 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[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

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/5ujm"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5ujm is ON HOLD
+==Structure of the active form of human Origin Recognition Complex and its ATPase motor module==
+<StructureSection load='5ujm' size='340' side='right' caption='[[5ujm]], [[Resolution|resolution]] 18.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ujm]] is a 5 chain structure. 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>
+</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=MG:MAGNESIUM+ION'>MG</scene></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=5ujm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ujm OCA], [http://pdbe.org/5ujm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ujm RCSB], [http://www.ebi.ac.uk/pdbsum/5ujm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ujm ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/ORC4_HUMAN ORC4_HUMAN]] Ear-patella-short stature syndrome. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/ORC1_HUMAN ORC1_HUMAN]] Ear-patella-short stature syndrome. The disease is caused by mutations affecting the gene represented in this entry.
+== Function ==
+[[http://www.uniprot.org/uniprot/ORC4_HUMAN 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.<ref>PMID:22427655</ref>  [[http://www.uniprot.org/uniprot/ORC1_HUMAN 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. [[http://www.uniprot.org/uniprot/ORC3_HUMAN 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.<ref>PMID:22427655</ref>  [[http://www.uniprot.org/uniprot/ORC2_HUMAN 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.<ref>PMID:22427655</ref> <ref>PMID:22935713</ref>  [[http://www.uniprot.org/uniprot/ORC5_HUMAN 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.
+<div style="background-color:#fffaf0;">
+== 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.
-Authors: Tocilj, A., On, K., 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.,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<ref>PMID:28112645</ref>
-Description: Structure of the active form of human Origin Recognition Complex and its ATPase motor module
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5ujm" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Elkayam, E]]
 [[Category: Joshua-Tor, L]]
+[[Category: Li, H]]
 [[Category: On, K]]
 [[Category: Stillman, B]]
-[[Category: Li, H]]
-[[Category: Elkayam, E]]
 [[Category: Sun, J]]
 [[Category: Tocilj, A]]
 [[Category: Yuan, Z]]
+[[Category: Atpase]]
+[[Category: Orc]]
+[[Category: Replication]]

5ujm

From Proteopedia

Revision as of 09:31, 10 March 2017

Structure of the active form of human Origin Recognition Complex and its ATPase motor module

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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