8gj2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:39, 17 October 2024) (edit) (undo)
 
Line 8: Line 8:
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8gj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gj2 OCA], [https://pdbe.org/8gj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gj2 RCSB], [https://www.ebi.ac.uk/pdbsum/8gj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gj2 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8gj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gj2 OCA], [https://pdbe.org/8gj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gj2 RCSB], [https://www.ebi.ac.uk/pdbsum/8gj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gj2 ProSAT]</span></td></tr>
</table>
</table>
-
== Function ==
+
<div style="background-color:#fffaf0;">
-
[https://www.uniprot.org/uniprot/HOLA_ECOLI HOLA_ECOLI] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The delta subunit seems to interact with the gamma subunit to transfer the beta subunit on the DNA.
+
== Publication Abstract from PubMed ==
 +
Ring-shaped DNA sliding clamps are essential for DNA replication and genome maintenance. Clamps need to be opened and chaperoned onto DNA by clamp loader complexes (CLCs). Detailed understanding of the mechanisms by which CLCs open and place clamps around DNA remains incomplete. Here, we present a series of six structures of the Escherichia coli CLC bound to an open or closed clamp prior to and after binding to a primer-template DNA, representing the most significant intermediates in the clamp loading process. We show that the ATP-bound CLC first binds to a clamp, then constricts to hold onto it. The CLC then expands to open the clamp with a gap large enough for double-stranded DNA to enter. Upon binding to DNA, the CLC constricts slightly, allowing clamp closing around DNA. These structures provide critical high-resolution snapshots of clamp loading by the E. coli CLC, revealing how the molecular machine works.
 +
 
 +
Structural characterisation of the complete cycle of sliding clamp loading in Escherichia coli.,Xu ZQ, Jergic S, Lo ATY, Pradhan AC, Brown SHJ, Bouwer JC, Ghodke H, Lewis PJ, Tolun G, Oakley AJ, Dixon NE Nat Commun. 2024 Sep 27;15(1):8372. doi: 10.1038/s41467-024-52623-9. PMID:39333521<ref>PMID:39333521</ref>
 +
 
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 8gj2" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

E. coli clamp loader with closed clamp on primed template DNA

PDB ID 8gj2

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools