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==Crystal structure of the DNA polymerase III subunit beta from Acinetobacter baumannii==
==Crystal structure of the DNA polymerase III subunit beta from Acinetobacter baumannii==
<StructureSection load='6ap4' size='340' side='right' caption='[[6ap4]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
<StructureSection load='6ap4' size='340' side='right'caption='[[6ap4]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ap4]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AP4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AP4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6ap4]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AP4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 2.95&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6amq|6amq]], [[6ams|6ams]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=6ap4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ap4 OCA], [http://pdbe.org/6ap4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ap4 RCSB], [http://www.ebi.ac.uk/pdbsum/6ap4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ap4 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=6ap4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ap4 OCA], [https://pdbe.org/6ap4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ap4 RCSB], [https://www.ebi.ac.uk/pdbsum/6ap4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ap4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/V5V7W3_ACIBA V5V7W3_ACIBA]] Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.[PIRNR:PIRNR000804]  
[https://www.uniprot.org/uniprot/V5V7W3_ACIBA V5V7W3_ACIBA] Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.[PIRNR:PIRNR000804]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial sliding clamps bind to DNA and act as protein-protein interaction hubs for several proteins involved in DNA replication and repair. The partner proteins all bind to a common pocket on sliding clamps via conserved linear peptide sequence motifs, which suggest the pocket as an attractive target for development of new antibiotics. Herein we report the X-ray crystal structures and biochemical characterization of beta sliding clamps from the Gram-negative pathogens Pseudomonas aeruginosa, Acinetobacter baumannii and Enterobacter cloacae. The structures reveal close similarity between the pathogen and Escherichia coli clamps and similar patterns of binding to linear clamp-binding motif peptides. The results suggest that linear motif-sliding clamp interactions are well conserved and an antibiotic targeting the sliding clamp should have broad-spectrum activity against Gram-negative pathogens.
 
Crystal structures and biochemical characterization of DNA sliding clamps from three Gram-negative bacterial pathogens.,McGrath AE, Martyn AP, Whittell LR, Dawes FE, Beck JL, Dixon NE, Kelso MJ, Oakley AJ J Struct Biol. 2018 Oct 23. pii: S1047-8477(18)30281-8. doi:, 10.1016/j.jsb.2018.10.008. PMID:30366028<ref>PMID:30366028</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ap4" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: McGrath, A E]]
[[Category: Acinetobacter baumannii]]
[[Category: Oakley, A J]]
[[Category: Large Structures]]
[[Category: Dna binding]]
[[Category: McGrath AE]]
[[Category: Dna directed dna polymerase activity]]
[[Category: Oakley AJ]]
[[Category: Transferase]]
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