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| | <StructureSection load='4p0y' size='340' side='right'caption='[[4p0y]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='4p0y' size='340' side='right'caption='[[4p0y]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4p0y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P0Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4p0y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P0Y 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">[[4edc|4edc]]</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=4p0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p0y OCA], [https://pdbe.org/4p0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p0y RCSB], [https://www.ebi.ac.uk/pdbsum/4p0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p0y 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=4p0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p0y OCA], [http://pdbe.org/4p0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p0y RCSB], [http://www.ebi.ac.uk/pdbsum/4p0y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p0y ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7BVV5_ENTFL Q7BVV5_ENTFL] |
| | <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: Enterococcus proteiformis thiercelin and jouhaud 1903]] | + | [[Category: Enterococcus faecalis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fercher, C]] | + | [[Category: Fercher C]] |
| - | [[Category: Goessweiner-mohr, N]] | + | [[Category: Goessweiner-mohr N]] |
| - | [[Category: Keller, W]] | + | [[Category: Keller W]] |
| - | [[Category: Conjugation]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dsdna binding]]
| + | |
| - | [[Category: Gram-positive]]
| + | |
| - | [[Category: Helix-turn-helix]]
| + | |
| Structural highlights
Function
Q7BVV5_ENTFL
Publication Abstract from PubMed
Conjugative transfer through type IV secretion multiprotein complexes is the most important means of spreading antimicrobial resistance. Plasmid pIP501, frequently found in clinical Enterococcus faecalis and Enterococcus faecium isolates, is the first Gram-positive (G+) conjugative plasmid for which self-transfer to Gram-negative (G-) bacteria has been demonstrated. The pIP501-encoded type IV secretion system (T4SS) protein TraN localizes to the cytoplasm and shows specific DNA binding. The specific DNA-binding site upstream of the pIP501 origin of transfer (oriT) was identified by a novel footprinting technique based on exonuclease digestion and sequencing, suggesting TraN to be an accessory protein of the pIP501 relaxase TraA. The structure of TraN was determined to 1.35 A resolution. It revealed an internal dimer fold with antiparallel beta-sheets in the centre and a helix-turn-helix (HTH) motif at both ends. Surprisingly, structurally related proteins (excisionases from T4SSs of G+ conjugative transposons and transcriptional regulators of the MerR family) resembling only one half of TraN were found. Thus, TraN may be involved in the early steps of pIP501 transfer, possibly triggering pIP501 TraA relaxase activity by recruiting the relaxosome to the assembled mating pore.
Structure of the double-stranded DNA-binding type IV secretion protein TraN from Enterococcus.,Goessweiner-Mohr N, Eder M, Hofer G, Fercher C, Arends K, Birner-Gruenberger R, Grohmann E, Keller W Acta Crystallogr D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2376-89. doi:, 10.1107/S1399004714014187. Epub 2014 Aug 29. PMID:25195751[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goessweiner-Mohr N, Eder M, Hofer G, Fercher C, Arends K, Birner-Gruenberger R, Grohmann E, Keller W. Structure of the double-stranded DNA-binding type IV secretion protein TraN from Enterococcus. Acta Crystallogr D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2376-89. doi:, 10.1107/S1399004714014187. Epub 2014 Aug 29. PMID:25195751 doi:http://dx.doi.org/10.1107/S1399004714014187
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