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==Crystal Structure of the E. coli clamp loader bound to Psi Peptide==
==Crystal Structure of the E. coli clamp loader bound to Psi Peptide==
<StructureSection load='3glh' size='340' side='right' caption='[[3glh]], [[Resolution|resolution]] 3.89&Aring;' scene=''>
<StructureSection load='3glh' size='340' side='right'caption='[[3glh]], [[Resolution|resolution]] 3.89&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3glh]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GLH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GLH FirstGlance]. <br>
<table><tr><td colspan='2'>[[3glh]] is a 15 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=3GLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GLH FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jr3|1jr3]], [[1xxh|1xxh]], [[1xxi|1xxi]], [[3glf|3glf]], [[3glg|3glg]], [[3gli|3gli]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.891&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">holA, b0640, JW0635 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), dnaX, dnaZ, dnaZX, b0470, JW0459 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), holB, b1099, JW1085 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3glh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3glh OCA], [https://pdbe.org/3glh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3glh RCSB], [https://www.ebi.ac.uk/pdbsum/3glh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3glh ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></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=3glh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3glh OCA], [http://pdbe.org/3glh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3glh RCSB], [http://www.ebi.ac.uk/pdbsum/3glh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3glh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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. [[http://www.uniprot.org/uniprot/HOLB_ECOLI HOLB_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. [[http://www.uniprot.org/uniprot/DPO3X_ECOLI DPO3X_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.  Isoform tau: serves as a scaffold to help in the dimerization of the core complex.  Isoform gamma: seems to interact with the delta subunit. to transfer the beta subunit on the DNA.  
[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3glh ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3glh ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Clamp loaders load sliding clamps onto primer-template DNA. The structure of the E. coli clamp loader bound to DNA reveals the formation of an ATP-dependent spiral of ATPase domains that tracks only the template strand, allowing recognition of both RNA and DNA primers. Unlike hexameric helicases, in which DNA translocation requires distinct conformations of the ATPase domains, the clamp loader spiral is symmetric and is set up to trigger release upon DNA recognition. Specificity for primed DNA arises from blockage of the end of the primer and accommodation of the emerging template along a surface groove. A related structure reveals how the psi protein, essential for coupling the clamp loader to single-stranded DNA-binding protein (SSB), binds to the clamp loader. By stabilizing a conformation of the clamp loader that is consistent with the ATPase spiral observed upon DNA binding, psi binding promotes the clamp-loading activity of the complex.
The mechanism of ATP-dependent primer-template recognition by a clamp loader complex.,Simonetta KR, Kazmirski SL, Goedken ER, Cantor AJ, Kelch BA, McNally R, Seyedin SN, Makino DL, O'Donnell M, Kuriyan J Cell. 2009 May 15;137(4):659-71. PMID:19450514<ref>PMID:19450514</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3glh" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[DNA polymerase|DNA polymerase]]
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: DNA-directed DNA polymerase]]
[[Category: Escherichia coli K-12]]
[[Category: Ecoli]]
[[Category: Large Structures]]
[[Category: Kazmirski, S L]]
[[Category: Kazmirski SL]]
[[Category: Kuriyan, J]]
[[Category: Kuriyan J]]
[[Category: Simonetta, K R]]
[[Category: Simonetta KR]]
[[Category: Atp-binding]]
[[Category: Clamp loader]]
[[Category: Dna replication]]
[[Category: Dna-directed dna polymerase]]
[[Category: Gamma complex]]
[[Category: Nucleotide-binding]]
[[Category: Nucleotidyltransferase]]
[[Category: PSI, Protein structure initiative]]
[[Category: Replication]]
[[Category: Transferase]]

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