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| | ==Structural insights into the unique single-stranded DNA binding mode of DNA processing protein A from Helicobacter pylori== | | ==Structural insights into the unique single-stranded DNA binding mode of DNA processing protein A from Helicobacter pylori== |
| - | <StructureSection load='4ljk' size='340' side='right' caption='[[4ljk]], [[Resolution|resolution]] 2.35Å' scene=''> | + | <StructureSection load='4ljk' size='340' side='right'caption='[[4ljk]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ljk]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LJK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LJK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ljk]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LJK FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ljl|4ljl]], [[4ljr|4ljr]]</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=4ljk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ljk OCA], [https://pdbe.org/4ljk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ljk RCSB], [https://www.ebi.ac.uk/pdbsum/4ljk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ljk ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP0333, HP_0333 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</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=4ljk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ljk OCA], [http://pdbe.org/4ljk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ljk RCSB], [http://www.ebi.ac.uk/pdbsum/4ljk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ljk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O25100_HELPY O25100_HELPY] |
| | <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: Campylobacter pylori]] | + | [[Category: Helicobacter pylori 26695]] |
| - | [[Category: Wang, W]] | + | [[Category: Large Structures]] |
| - | [[Category: Dna binding protein]] | + | [[Category: Wang W]] |
| - | [[Category: Dna processg a domain]]
| + | |
| - | [[Category: Natural recombination mediating protein]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Selenium derivative]]
| + | |
| - | [[Category: Ssdna binding]]
| + | |
| Structural highlights
Function
O25100_HELPY
Publication Abstract from PubMed
Natural transformation (NT) in bacteria is a complex process, including binding, uptake, transport and recombination of exogenous DNA into the chromosome, consequently generating genetic diversity and driving evolution. DNA processing protein A (DprA), which is distributed among virtually all bacterial species, is involved in binding to the internalized single-stranded DNA (ssDNA) and promoting the loading of RecA on ssDNA during NTs. Here we present the structures of DNA_processg_A (DprA) domain of the Helicobacter pylori DprA (HpDprA) and its complex with an ssDNA at 2.20 and 1.80 A resolutions, respectively. The complex structure revealed for the first time how the conserved DprA domain binds to ssDNA. Based on structural comparisons and binding assays, a unique ssDNA-binding mode is proposed: the dimer of HpDprA binds to ssDNA through two small, positively charged binding pockets of the DprA domains with classical Rossmann folds and the key residue Arg52 is re-oriented to 'open' the pocket in order to accommodate one of the bases of ssDNA, thus enabling HpDprA to grasp substrate with high affinity. This mode is consistent with the oligomeric composition of the complex as shown by electrophoretic mobility-shift assays and static light scattering measurements, but differs from the direct polymeric complex of Streptococcus pneumoniae DprA-ssDNA.
Structural insights into the unique single-stranded DNA-binding mode of Helicobacter pylori DprA.,Wang W, Ding J, Zhang Y, Hu Y, Wang DC Nucleic Acids Res. 2013 Dec 24. PMID:24369431[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang W, Ding J, Zhang Y, Hu Y, Wang DC. Structural insights into the unique single-stranded DNA-binding mode of Helicobacter pylori DprA. Nucleic Acids Res. 2013 Dec 24. PMID:24369431 doi:http://dx.doi.org/10.1093/nar/gkt1334
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