6ap4
From Proteopedia
(Difference between revisions)
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<StructureSection load='6ap4' size='340' side='right' caption='[[6ap4]], [[Resolution|resolution]] 2.95Å' scene=''> | <StructureSection load='6ap4' size='340' side='right' caption='[[6ap4]], [[Resolution|resolution]] 2.95Å' 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 [http://en.wikipedia.org/wiki/Aciba Aciba]. 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> |
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6amq|6amq]], [[6ams|6ams]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnaN, A7M79_16225, A7M90_19325, A7N09_15145, AB895_1514, ABUW_0002, APD06_07570, APD31_16715, AZE33_00010, B4R90_12040, B9X95_11540, BGC29_18735, BWP00_10155, CAS83_08665, CBI29_00019, CEB38_18810, IX87_14440, LV38_03508 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=470 ACIBA])</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'>[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> | ||
</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] | [[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] | ||
| + | <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®/PubMed®, 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|DNA polymerase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Aciba]] | ||
[[Category: McGrath, A E]] | [[Category: McGrath, A E]] | ||
[[Category: Oakley, A J]] | [[Category: Oakley, A J]] | ||
Revision as of 12:37, 7 November 2018
Crystal structure of the DNA polymerase III subunit beta from Acinetobacter baumannii
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