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==SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN OF THE TRAM PROTEIN== | ==SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN OF THE TRAM PROTEIN== | ||
<StructureSection load='1dp3' size='340' side='right' caption='[[1dp3 | <StructureSection load='1dp3' size='340' side='right'caption='[[1dp3]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dp3]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1dp3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DP3 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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'>[https://proteopedia.org/fgij/fg.htm?mol=1dp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dp3 OCA], [https://pdbe.org/1dp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dp3 RCSB], [https://www.ebi.ac.uk/pdbsum/1dp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dp3 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TRAM2_ECOLX TRAM2_ECOLX] 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. Probably autoregulates its own expression. Plasmid specificity is conferred by the TraD-TraM pair (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dp3_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/1dp3_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dp3 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 23: | Line 27: | ||
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 1dp3" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 28: | Line 33: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Bermel | [[Category: Large Structures]] | ||
[[Category: Hoegenauer | [[Category: Bermel W]] | ||
[[Category: Koraimann | [[Category: Hoegenauer G]] | ||
[[Category: Plugariu | [[Category: Koraimann G]] | ||
[[Category: Prytulla | [[Category: Plugariu C]] | ||
[[Category: Sterk | [[Category: Prytulla S]] | ||
[[Category: Stockner | [[Category: Sterk H]] | ||
[[Category: Stockner T]] | |||
Latest revision as of 11:24, 22 May 2024
SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN OF THE TRAM PROTEINSOLUTION STRUCTURE OF THE DNA BINDING DOMAIN OF THE TRAM PROTEIN
Structural highlights
FunctionTRAM2_ECOLX 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. Probably autoregulates its own expression. Plasmid specificity is conferred by the TraD-TraM pair (By similarity). 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 PubMedThe solution structure of the DNA-binding domain of the TraM protein, an essential component of the DNA transfer machinery of the conjugative resistance plasmid R1, is presented. The structure has been determined using homonuclear 2-dimensional NMR spectroscopy as well as 15N labeled heteronuclear 2- and 3-dimensional NMR spectroscopy. It turns out that the solution structure of the DNA binding domain of the TraM protein is globular and dominantly helical. The very first amino acids of the N-terminus are unstructured. Solution structure of the DNA-binding domain of TraM.,Stockner T, Plugariu C, Koraimann G, Hogenauer G, Bermel W, Prytulla S, Sterk H Biochemistry. 2001 Mar 20;40(11):3370-7. PMID:11258958[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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