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| <StructureSection load='6iud' size='340' side='right'caption='[[6iud]], [[Resolution|resolution]] 2.51Å' scene=''> | | <StructureSection load='6iud' size='340' side='right'caption='[[6iud]], [[Resolution|resolution]] 2.51Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6iud]] is a 6 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=6IUD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IUD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6iud]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IUD FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 2.506Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP_1139 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=6iud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iud OCA], [http://pdbe.org/6iud PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iud RCSB], [http://www.ebi.ac.uk/pdbsum/6iud PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iud 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=6iud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iud OCA], [https://pdbe.org/6iud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iud RCSB], [https://www.ebi.ac.uk/pdbsum/6iud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iud ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/O25759_HELPY O25759_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: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Chu, C H]] | + | [[Category: Synthetic construct]] |
- | [[Category: Sun, Y J]] | + | [[Category: Chu CH]] |
- | [[Category: Yen, C Y]] | + | [[Category: Sun YJ]] |
- | [[Category: Dna binding protein]] | + | [[Category: Yen CY]] |
- | [[Category: Dna binding protein-dna complex]]
| + | |
- | [[Category: Partition protein]]
| + | |
| Structural highlights
Function
O25759_HELPY
Publication Abstract from PubMed
ParABS, an important DNA partitioning process in chromosome segregation, includes ParA (an ATPase), ParB (a parS binding protein) and parS (a centromere-like DNA). The homologous proteins of ParA and ParB in Helicobacter pylori are HpSoj and HpSpo0J, respectively. We analyzed the ATPase activity of HpSoj and found that it is enhanced by both DNA and HpSpo0J. Crystal structures of HpSoj and its DNA complexes revealed a typical ATPase fold and that it is dimeric. DNA binding by HpSoj is promoted by ATP. The HpSoj-ATP-DNA complex non-specifically binds DNA through a continuous basic binding patch formed by lysine residues, with a single DNA-binding site. This complex exhibits a DNA-binding adept state with an active ATP-bound conformation, whereas the HpSoj-ADP-DNA complex may represent a transient DNA-bound state. Based on structural comparisons, HpSoj exhibits a similar DNA binding surface to the bacterial ParA superfamily, but the archaeal ParA superfamily exhibits distinct non-specific DNA-binding via two DNA-binding sites. We detected the HpSpo0J-HpSoj-DNA complex by electron microscopy and show that this nucleoid-adaptor complex (NAC) is formed through HpSoj and HpSpo0J interaction and parS DNA binding. NAC formation is promoted by HpSoj participation and specific parS DNA facilitation.
Crystal structures of HpSoj-DNA complexes and the nucleoid-adaptor complex formation in chromosome segregation.,Chu CH, Yen CY, Chen BW, Lin MG, Wang LH, Tang KZ, Hsiao CD, Sun YJ Nucleic Acids Res. 2018 Dec 14. pii: 5245442. doi: 10.1093/nar/gky1251. PMID:30544248[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chu CH, Yen CY, Chen BW, Lin MG, Wang LH, Tang KZ, Hsiao CD, Sun YJ. Crystal structures of HpSoj-DNA complexes and the nucleoid-adaptor complex formation in chromosome segregation. Nucleic Acids Res. 2018 Dec 14. pii: 5245442. doi: 10.1093/nar/gky1251. PMID:30544248 doi:http://dx.doi.org/10.1093/nar/gky1251
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