|
|
(One intermediate revision not shown.) |
Line 3: |
Line 3: |
| <StructureSection load='2ccz' size='340' side='right'caption='[[2ccz]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='2ccz' size='340' side='right'caption='[[2ccz]], [[Resolution|resolution]] 2.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2ccz]] is a 3 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=2CCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CCZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ccz]] is a 3 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=2CCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CCZ FirstGlance]. <br> |
- | </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=2ccz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ccz OCA], [http://pdbe.org/2ccz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ccz RCSB], [http://www.ebi.ac.uk/pdbsum/2ccz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ccz ProSAT]</span></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]] 2.7Å</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=2ccz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ccz OCA], [https://pdbe.org/2ccz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ccz RCSB], [https://www.ebi.ac.uk/pdbsum/2ccz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ccz ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [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> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
Line 29: |
Line 32: |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Hsiao, C D]] | + | [[Category: Hsiao C-D]] |
- | [[Category: Hsu, C H]] | + | [[Category: Hsu C-H]] |
- | [[Category: Huang, C Y]] | + | [[Category: Huang C-Y]] |
- | [[Category: Sun, Y J]] | + | [[Category: Sun Y-J]] |
- | [[Category: Wu, H N]] | + | [[Category: Wu H-N]] |
- | [[Category: Dna recombination]]
| + | |
- | [[Category: Dna repair]]
| + | |
- | [[Category: Dna replication]]
| + | |
- | [[Category: Dna-protein complex]]
| + | |
- | [[Category: Dna-replication complex]]
| + | |
- | [[Category: Dna/replication]]
| + | |
- | [[Category: Prib]]
| + | |
- | [[Category: Primosome]]
| + | |
- | [[Category: Single-stranded dna]]
| + | |
- | [[Category: Ssdna]]
| + | |
| 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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
PriB is a primosomal protein required for replication restart in Escherichia coli. PriB stimulates PriA helicase activity via interaction with single-stranded DNA (ssDNA), but the molecular details of this interaction remain unclear. Here, we report the crystal structure of PriB complexed with a 15 bases oligonucleotide (dT15) at 2.7 A resolution. PriB shares structural similarity with the E.coli ssDNA-binding protein (EcoSSB). However, the structure of the PriB-dT15 complex reveals that PriB binds ssDNA differently. Results from filter-binding assays show that PriB-ssDNA interaction is salt-sensitive and cooperative. Mutational analysis suggests that the loop L45 plays an important role in ssDNA binding. Based on the crystal structure and biochemical analyses, we propose a cooperative mechanism for the binding of PriB to ssDNA and a model for the assembly of the PriA-PriB-ssDNA complex. This report presents the first structure of a replication restart primosomal protein complexed with DNA, and a novel model that explains the interactions between a dimeric oligonucleotide-binding-fold protein and ssDNA.
Complexed crystal structure of replication restart primosome protein PriB reveals a novel single-stranded DNA-binding mode.,Huang CY, Hsu CH, Sun YJ, Wu HN, Hsiao CD Nucleic Acids Res. 2006;34(14):3878-86. Epub 2006 Aug 9. PMID:16899446[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
- ↑ Huang CY, Hsu CH, Sun YJ, Wu HN, Hsiao CD. Complexed crystal structure of replication restart primosome protein PriB reveals a novel single-stranded DNA-binding mode. Nucleic Acids Res. 2006;34(14):3878-86. Epub 2006 Aug 9. PMID:16899446 doi:http://dx.doi.org/10.1093/nar/gkl536
|