| Structural highlights
6ap4 is a 16 chain structure with sequence from Aciba. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | |
| Related: | 6amq, 6ams |
| Gene: | 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 (ACIBA) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[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]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ McGrath AE, Martyn AP, Whittell LR, Dawes FE, Beck JL, Dixon NE, Kelso MJ, Oakley AJ. Crystal structures and biochemical characterization of DNA sliding clamps from three Gram-negative bacterial pathogens. J Struct Biol. 2018 Oct 23. pii: S1047-8477(18)30281-8. doi:, 10.1016/j.jsb.2018.10.008. PMID:30366028 doi:http://dx.doi.org/10.1016/j.jsb.2018.10.008
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