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| | ==Crystal structure of apeThermo-DBP-RP2== | | ==Crystal structure of apeThermo-DBP-RP2== |
| - | <StructureSection load='4psn' size='340' side='right' caption='[[4psn]], [[Resolution|resolution]] 2.05Å' scene=''> | + | <StructureSection load='4psn' size='340' side='right'caption='[[4psn]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4psn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aerpe Aerpe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PSN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PSN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4psn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix_K1 Aeropyrum pernix K1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PSN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PSN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4psn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4psn OCA], [https://pdbe.org/4psn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4psn RCSB], [https://www.ebi.ac.uk/pdbsum/4psn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4psn ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4psl|4psl]], [[4psm|4psm]], [[4pso|4pso]]</td></tr>
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| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APE_1866.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272557 AERPE])</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=4psn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4psn OCA], [http://pdbe.org/4psn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4psn RCSB], [http://www.ebi.ac.uk/pdbsum/4psn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4psn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9YAS7_AERPE Q9YAS7_AERPE] |
| | <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: Aerpe]] | + | [[Category: Aeropyrum pernix K1]] |
| - | [[Category: Eppers, D]] | + | [[Category: Large Structures]] |
| - | [[Category: Gahlei, H]] | + | [[Category: Eppers D]] |
| - | [[Category: Loll, B]] | + | [[Category: Gahlei H]] |
| - | [[Category: Moeller, H von]] | + | [[Category: Loll B]] |
| - | [[Category: Wahl, M C]] | + | [[Category: Wahl MC]] |
| - | [[Category: Dna binding protein]] | + | [[Category: Von Moeller H]] |
| - | [[Category: Ssdna binding protein]]
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| Structural highlights
Function
Q9YAS7_AERPE
Publication Abstract from PubMed
Instead of a classical single-stranded deoxyribonuleic acid (DNA)-binding protein (SSB), some hyperthermophilic crenarchaea harbor a non-canonical SSB termed ThermoDBP. Two related but poorly characterized groups of proteins, which share the ThermoDBP N-terminal DNA-binding domain, have a broader phylogenetic distribution and co-exist with ThermoDBPs and/or other SSBs. We have investigated the nucleic acid binding properties and crystal structures of representatives of these groups of ThermoDBP-related proteins (ThermoDBP-RPs) 1 and 2. ThermoDBP-RP 1 and 2 oligomerize by different mechanisms and only ThermoDBP-RP2 exhibits strong single-stranded DNA affinity in vitro. A crystal structure of ThermoDBP-RP2 in complex with DNA reveals how the NTD common to ThermoDBPs and ThermoDBP-RPs can contact the nucleic acid in a manner that allows a symmetric homotetrameric protein complex to bind single-stranded DNA molecules asymmetrically. While single-stranded DNA wraps around the surface or binds along channels of previously investigated SSBs, it traverses an internal, intersubunit tunnel system of a ThermoDBP-RP2 tetramer. Our results indicate that some archaea have acquired special SSBs for genome maintenance in particularly challenging environments.
Entrapment of DNA in an intersubunit tunnel system of a single-stranded DNA-binding protein.,Ghalei H, Moeller HV, Eppers D, Sohmen D, Wilson DN, Loll B, Wahl MC Nucleic Acids Res. 2014 Apr 17. PMID:24744237[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ghalei H, Moeller HV, Eppers D, Sohmen D, Wilson DN, Loll B, Wahl MC. Entrapment of DNA in an intersubunit tunnel system of a single-stranded DNA-binding protein. Nucleic Acids Res. 2014 Apr 17. PMID:24744237 doi:http://dx.doi.org/10.1093/nar/gku259
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