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| | <StructureSection load='3d8a' size='340' side='right'caption='[[3d8a]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='3d8a' size='340' side='right'caption='[[3d8a]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3d8a]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D8A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3d8a]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D8A FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2g7o|2g7o]]</div></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]] 2.55Å</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=3d8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d8a OCA], [https://pdbe.org/3d8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d8a RCSB], [https://www.ebi.ac.uk/pdbsum/3d8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d8a 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=3d8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d8a OCA], [https://pdbe.org/3d8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d8a RCSB], [https://www.ebi.ac.uk/pdbsum/3d8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d8a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TRAM1_ECOLI TRAM1_ECOLI]] Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut in the origin of transfer by TraI, at the nic site. Cooperatively binds 3 regions in the F plasmid oriT locus; 2 are required for autoregulation while the other is required for plasmid transfer. Bends oriT DNA less than 50 degrees. Plasmid specificity is conferred by the TraD-TraM pair.<ref>PMID:1479887</ref> <ref>PMID:8736534</ref> <ref>PMID:11875064</ref> <ref>PMID:17238924</ref>
| + | [https://www.uniprot.org/uniprot/TRAM1_ECOLI TRAM1_ECOLI] Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut in the origin of transfer by TraI, at the nic site. Cooperatively binds 3 regions in the F plasmid oriT locus; 2 are required for autoregulation while the other is required for plasmid transfer. Bends oriT DNA less than 50 degrees. Plasmid specificity is conferred by the TraD-TraM pair.<ref>PMID:1479887</ref> <ref>PMID:8736534</ref> <ref>PMID:11875064</ref> <ref>PMID:17238924</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Edwards, R A]] | + | [[Category: Edwards RA]] |
| - | [[Category: Glover, J N.M]] | + | [[Category: Glover JNM]] |
| - | [[Category: Lu, J]] | + | [[Category: Lu J]] |
| - | [[Category: Wong, J J]] | + | [[Category: Wong JJ]] |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Conjugation]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Inner membrane]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Protein complex]]
| + | |
| - | [[Category: Trad c-terminal peptide]]
| + | |
| - | [[Category: Tram tetramerization domain]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| Structural highlights
Function
TRAM1_ECOLI Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut in the origin of transfer by TraI, at the nic site. Cooperatively binds 3 regions in the F plasmid oriT locus; 2 are required for autoregulation while the other is required for plasmid transfer. Bends oriT DNA less than 50 degrees. Plasmid specificity is conferred by the TraD-TraM pair.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
F plasmid-mediated bacterial conjugation requires interactions between a relaxosome component, TraM, and the coupling protein TraD, a hexameric ring ATPase that forms the cytoplasmic face of the conjugative pore. Here we present the crystal structure of the C-terminal tail of TraD bound to the TraM tetramerization domain, the first structural evidence of relaxosome-coupling protein interactions. The structure reveals the TraD C-terminal peptide bound to each of four symmetry-related grooves on the surface of the TraM tetramer. Extensive protein-protein interactions were observed between the two proteins. Mutational analysis indicates that these interactions are specific and required for efficient F conjugation in vivo. Our results suggest that specific interactions between the C-terminal tail of TraD and the TraM tetramerization domain might lead to more generalized interactions that stabilize the relaxosome-coupling protein complex in preparation for conjugative DNA transfer.
Structural basis of specific TraD-TraM recognition during F plasmid-mediated bacterial conjugation.,Lu J, Wong JJ, Edwards RA, Manchak J, Frost LS, Glover JN Mol Microbiol. 2008 Oct;70(1):89-99. Epub 2008 Aug 19. PMID:18717787[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Di Laurenzio L, Frost LS, Paranchych W. The TraM protein of the conjugative plasmid F binds to the origin of transfer of the F and ColE1 plasmids. Mol Microbiol. 1992 Oct;6(20):2951-9. PMID:1479887
- ↑ Penfold SS, Simon J, Frost LS. Regulation of the expression of the traM gene of the F sex factor of Escherichia coli. Mol Microbiol. 1996 May;20(3):549-58. PMID:8736534
- ↑ Fekete RA, Frost LS. Characterizing the DNA contacts and cooperative binding of F plasmid TraM to its cognate sites at oriT. J Biol Chem. 2002 May 10;277(19):16705-11. Epub 2002 Mar 1. PMID:11875064 doi:http://dx.doi.org/10.1074/jbc.M111682200
- ↑ Ragonese H, Haisch D, Villareal E, Choi JH, Matson SW. The F plasmid-encoded TraM protein stimulates relaxosome-mediated cleavage at oriT through an interaction with TraI. Mol Microbiol. 2007 Feb;63(4):1173-84. PMID:17238924 doi:http://dx.doi.org/10.1111/j.1365-2958.2006.05576.x
- ↑ Lu J, Wong JJ, Edwards RA, Manchak J, Frost LS, Glover JN. Structural basis of specific TraD-TraM recognition during F plasmid-mediated bacterial conjugation. Mol Microbiol. 2008 Oct;70(1):89-99. Epub 2008 Aug 19. PMID:18717787 doi:10.1111/j.1365-2958.2008.06391.x
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