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| | <StructureSection load='5wqv' size='340' side='right'caption='[[5wqv]], [[Resolution|resolution]] 1.97Å' scene=''> | | <StructureSection load='5wqv' size='340' side='right'caption='[[5wqv]], [[Resolution|resolution]] 1.97Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wqv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobw Ecobw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WQV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wqv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BW2952 Escherichia coli BW2952]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WQV FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">priB, BWG_3913 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=595496 ECOBW])</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]] 1.97Å</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=5wqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wqv OCA], [http://pdbe.org/5wqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wqv RCSB], [http://www.ebi.ac.uk/pdbsum/5wqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wqv 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=5wqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wqv OCA], [https://pdbe.org/5wqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wqv RCSB], [https://www.ebi.ac.uk/pdbsum/5wqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wqv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PRIB_ECOBW PRIB_ECOBW]] Binds single-stranded DNA at the primosome assembly site (PAS). During primosome assembly it facilitates the complex formation between PriA and DnaT. | + | [https://www.uniprot.org/uniprot/PRIB_ECOLI PRIB_ECOLI] Binds single-stranded DNA at the primosome assembly site (PAS). During primosome assembly it facilitates the complex formation between PriA and DnaT.<ref>PMID:1856227</ref> <ref>PMID:1646811</ref> <ref>PMID:8366072</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecobw]] | + | [[Category: Escherichia coli BW2952]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Abe, Y]] | + | [[Category: Abe Y]] |
| - | [[Category: Fujiyama, S]] | + | [[Category: Fujiyama S]] |
| - | [[Category: Katayama, T]] | + | [[Category: Katayama T]] |
| - | [[Category: Shiroishi, M]] | + | [[Category: Shiroishi M]] |
| - | [[Category: Ueda, T]] | + | [[Category: Ueda T]] |
| - | [[Category: Bacterial dna replication]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Ob-fold]]
| + | |
| - | [[Category: S55a mutant]]
| + | |
| Structural highlights
Function
PRIB_ECOLI Binds single-stranded DNA at the primosome assembly site (PAS). During primosome assembly it facilitates the complex formation between PriA and DnaT.[1] [2] [3]
Publication Abstract from PubMed
When the replisome collapses at a DNA damage site, a sequence-independent replication restart system is required. In Escherichia coli, PriA, PriB, and DnaT assemble in an orderly fashion at the stalled replication fork and achieve the reloading of the replisome. PriB-DnaT interaction is considered a significant step in the replication restart. In this study, we examined the contribution of the residues Ser20, His26 and Ser55, which are located on the PriB dimer interface. These residues are proximal to Glu39 and Arg44, which are important for PriB-DnaT interaction. Mutational analyses revealed that His26 and Ser20 of PriB are important for the interaction with DnaT, and that the Ser55 residue of PriB might have a role in negatively regulating the DnaT binding. These residues are involved in not only the interaction between PriB and DnaT but also the dissociation of single-stranded DNA (ssDNA) from the PriB-ssDNA complex due to DnaT binding. Moreover, NMR study indicates that the region Asp66-Glu76 on the linker between DnaT domains is involved in the interaction with wild-type PriB. These findings provide significant information about the molecular mechanism underlying replication restart in bacteria.
Insight into the interaction between PriB and DnaT on bacterial DNA replication restart: Significance of the residues on PriB dimer interface and highly acidic region on DnaT.,Fujiyama S, Abe Y, Shiroishi M, Ikeda Y, Ueda T Biochim Biophys Acta Proteins Proteom. 2019 Apr;1867(4):367-375. doi:, 10.1016/j.bbapap.2019.01.008. Epub 2019 Jan 16. PMID:30659961[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zavitz KH, DiGate RJ, Marians KJ. The priB and priC replication proteins of Escherichia coli. Genes, DNA sequence, overexpression, and purification. J Biol Chem. 1991 Jul 25;266(21):13988-95. PMID:1856227
- ↑ Allen GC Jr, Kornberg A. The priB gene encoding the primosomal replication n protein of Escherichia coli. J Biol Chem. 1991 Jun 25;266(18):11610-3. PMID:1646811
- ↑ Allen GC Jr, Kornberg A. Assembly of the primosome of DNA replication in Escherichia coli. J Biol Chem. 1993 Sep 15;268(26):19204-9. PMID:8366072
- ↑ Fujiyama S, Abe Y, Shiroishi M, Ikeda Y, Ueda T. Insight into the interaction between PriB and DnaT on bacterial DNA replication restart: Significance of the residues on PriB dimer interface and highly acidic region on DnaT. Biochim Biophys Acta Proteins Proteom. 2019 Apr;1867(4):367-375. doi:, 10.1016/j.bbapap.2019.01.008. Epub 2019 Jan 16. PMID:30659961 doi:http://dx.doi.org/10.1016/j.bbapap.2019.01.008
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