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| ==NMR Structure of ParG symmetric dimer== | | ==NMR Structure of ParG symmetric dimer== |
- | <StructureSection load='1p94' size='340' side='right' caption='[[1p94]], [[NMR_Ensembles_of_Models | 11 NMR models]]' scene=''> | + | <StructureSection load='1p94' size='340' side='right'caption='[[1p94]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1p94]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P94 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P94 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1p94]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P94 FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">parG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28901 Salmonella enterica])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1p94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p94 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p94 RCSB], [http://www.ebi.ac.uk/pdbsum/1p94 PDBsum]</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=1p94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p94 OCA], [https://pdbe.org/1p94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p94 RCSB], [https://www.ebi.ac.uk/pdbsum/1p94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p94 ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q9KJ82_SALNE Q9KJ82_SALNE] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| </div> | | </div> |
| + | <div class="pdbe-citations 1p94" style="background-color:#fffaf0;"></div> |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| + | [[Category: Large Structures]] |
| [[Category: Salmonella enterica]] | | [[Category: Salmonella enterica]] |
- | [[Category: Barilla, D]] | + | [[Category: Barilla D]] |
- | [[Category: Golovanov, A P]] | + | [[Category: Golovanov AP]] |
- | [[Category: Golovanova, M]] | + | [[Category: Golovanova M]] |
- | [[Category: Hayes, F]] | + | [[Category: Hayes F]] |
- | [[Category: Lian, L Y]] | + | [[Category: Lian LY]] |
- | [[Category: Cell cycle]]
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- | [[Category: Dimer]]
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- | [[Category: Dna binding]]
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- | [[Category: Ribbon-helix-helix]]
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| Structural highlights
Function
Q9KJ82_SALNE
Publication Abstract from PubMed
The ParG protein (8.6 kDa) is an essential component of the DNA partition complex of multidrug resistance plasmid TP228. ParG is a dimer in solution, interacts with DNA sequences upstream of the parFG genes and also with the ParF partition protein both in the absence and presence of target DNA. Here, the solution nuclear magnetic resonance structure of ParG is reported. The ParG dimer is composed of a folded domain formed by two closely intertwined C-terminal parts (residues 33-76), and two highly mobile tails consisting of N-terminal regions (residues 1-32). The folded part of ParG has the ribbon-helix-helix (RHH) architecture similar to that of the Arc/MetJ superfamily of DNA-binding transcriptional repressors, although the primary sequence similarity is very low. ParG interacts with DNA predominantly via its folded domain; this interaction is coupled with ParG oligomerization. The dimeric RHH structure of ParG suggests that it binds to DNA by inserting the double-stranded beta-sheet into the major groove of DNA, in a manner similar to transcriptional repressors from the Arc/MetJ superfamily, and that ParG can function as a transcriptional repressor itself. A new classification of proteins belonging to the Arc/MetJ superfamily and ParG homologues is proposed, based on the location of a conserved positively charged residue at either the beginning or at the end of the beta-strand which forms part of the DNA recognition motif.
ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure.,Golovanov AP, Barilla D, Golovanova M, Hayes F, Lian LY Mol Microbiol. 2003 Nov;50(4):1141-53. PMID:14622405[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Golovanov AP, Barilla D, Golovanova M, Hayes F, Lian LY. ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure. Mol Microbiol. 2003 Nov;50(4):1141-53. PMID:14622405
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