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==cryo-EM structure of the E. coli replicative DNA polymerase complex in DNA free state (DNA polymerase III alpha, beta, epsilon, tau complex)==
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== Structural highlights ==
<table><tr><td colspan='2'>[[5fku]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FKU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.34&#8491;</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=5fku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fku OCA], [https://pdbe.org/5fku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fku RCSB], [https://www.ebi.ac.uk/pdbsum/5fku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fku ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/DPO3A_ECOLI DPO3A_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 alpha chain is the DNA polymerase.
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== Publication Abstract from PubMed ==
The replicative DNA polymerase PolIIIalpha from E. coli is a uniquely fast and processive enzyme. For its activity it relies on the DNA sliding clamp beta, the proofreading exonuclease epsilon and the C-terminal domain of the clamp loader subunit tau. Due to the dynamic nature of the four-protein complex it has long been refractory to structural characterization. Here we present the 8 A resolution cryo-electron microscopy structures of DNA-bound and DNA-free states of the PolIII-clamp-exonuclease-tauc complex. The structures show how the polymerase is tethered to the DNA through multiple contacts with the clamp and exonuclease. A novel contact between the polymerase and clamp is made in the DNA bound state, facilitated by a large movement of the polymerase tail domain and tauc. These structures provide crucial insights into the organization of the catalytic core of the replisome and form an important step towards determining the structure of the complete holoenzyme.

cryo-EM structures of the E. coli replicative DNA polymerase reveal dynamic interactions with clamp, exonuclease and tau.,Fernandez-Leiro R, Conrad J, Scheres SH, Lamers MH Elife. 2015 Oct 24;4. pii: e11134. doi: 10.7554/eLife.11134. PMID:26499492<ref>PMID:26499492</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
== References ==
<references/>
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Conrad J]]
[[Category: Fernandez-Leiro R]]
[[Category: Lamers MH]]
[[Category: Scheres SHW]]