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| <StructureSection load='4ou6' size='340' side='right'caption='[[4ou6]], [[Resolution|resolution]] 1.96Å' scene=''> | | <StructureSection load='4ou6' size='340' side='right'caption='[[4ou6]], [[Resolution|resolution]] 1.96Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4ou6]] is a 6 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=4OU6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OU6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ou6]] is a 6 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=4OU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OU6 FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ou7|4ou7]]</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]] 1.96Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnaT, b4362, JW4326 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4ou6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ou6 OCA], [https://pdbe.org/4ou6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ou6 RCSB], [https://www.ebi.ac.uk/pdbsum/4ou6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ou6 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=4ou6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ou6 OCA], [http://pdbe.org/4ou6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ou6 RCSB], [http://www.ebi.ac.uk/pdbsum/4ou6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ou6 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/DNAT_ECOLI DNAT_ECOLI]] This protein is required for primosome-dependent normal DNA replication; it is also involved in inducing stable DNA replication during SOS response. It forms, in concert with DnaB protein and other prepriming proteins DnaC, N, N', N'' a prepriming protein complex on the specific site of the template DNA recognized by protein N'.[HAMAP-Rule:MF_01061] | + | [https://www.uniprot.org/uniprot/DNAT_ECOLI DNAT_ECOLI] This protein is required for primosome-dependent normal DNA replication; it is also involved in inducing stable DNA replication during SOS response. It forms, in concert with DnaB protein and other prepriming proteins DnaC, N, N', N'' a prepriming protein complex on the specific site of the template DNA recognized by protein N'.[HAMAP-Rule:MF_01061] |
| <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: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Chen, P]] | + | [[Category: Chen P]] |
- | [[Category: Li, X]] | + | [[Category: Li X]] |
- | [[Category: Liu, Z]] | + | [[Category: Liu Z]] |
- | [[Category: Niu, L]] | + | [[Category: Niu L]] |
- | [[Category: Teng, M]] | + | [[Category: Teng M]] |
- | [[Category: Dna binding]]
| + | |
- | [[Category: Replication-dna complex]]
| + | |
| Structural highlights
Function
DNAT_ECOLI This protein is required for primosome-dependent normal DNA replication; it is also involved in inducing stable DNA replication during SOS response. It forms, in concert with DnaB protein and other prepriming proteins DnaC, N, N', N a prepriming protein complex on the specific site of the template DNA recognized by protein N'.[HAMAP-Rule:MF_01061]
Publication Abstract from PubMed
DnaT is a primosomal protein that is required for the stalled replication fork restart in Escherichia coli. As an adapter, DnaT mediates the PriA-PriB-ssDNA ternary complex and the DnaB/C complex. However, the fundamental function of DnaT during PriA-dependent primosome assembly is still a black box. Here, we report the 2.83 A DnaT84-153-dT10 ssDNA complex structure, which reveals a novel three-helix bundle single-stranded DNA binding mode. Based on binding assays and negative-staining electron microscopy results, we found that DnaT can bind to phiX 174 ssDNA to form nucleoprotein filaments for the first time, which indicates that DnaT might function as a scaffold protein during the PriA-dependent primosome assembly. In combination with biochemical analysis, we propose a cooperative mechanism for the binding of DnaT to ssDNA and a possible model for the assembly of PriA-PriB-ssDNA-DnaT complex that sheds light on the function of DnaT during the primosome assembly and stalled replication fork restart. This report presents the first structure of the DnaT C-terminal complex with ssDNA and a novel model that explains the interactions between the three-helix bundle and ssDNA.
Crystal structure of DnaT84-153-dT10 ssDNA complex reveals a novel single-stranded DNA binding mode.,Liu Z, Chen P, Wang X, Cai G, Niu L, Teng M, Li X Nucleic Acids Res. 2014 Jul 22. pii: gku633. PMID:25053836[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu Z, Chen P, Wang X, Cai G, Niu L, Teng M, Li X. Crystal structure of DnaT84-153-dT10 ssDNA complex reveals a novel single-stranded DNA binding mode. Nucleic Acids Res. 2014 Jul 22. pii: gku633. PMID:25053836 doi:http://dx.doi.org/10.1093/nar/gku633
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