1dvo: Difference between revisions

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 <StructureSection load='1dvo' size='340' side='right'caption='[[1dvo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dvo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DVO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1dvo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DVO FirstGlance]. <br>
-</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=1dvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dvo OCA], [https://pdbe.org/1dvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dvo RCSB], [https://www.ebi.ac.uk/pdbsum/1dvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dvo ProSAT]</span></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&#8491;</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=1dvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dvo OCA], [https://pdbe.org/1dvo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dvo RCSB], [https://www.ebi.ac.uk/pdbsum/1dvo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dvo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/FINO3_ECOLX FINO3_ECOLX]] One of the components on the FinOP fertility inhibition complex, which inhibits the expression of traJ gene, which in turn regulates the expression of some 20 transfer genes. The transfer genes are responsible for the process, called conjugal transfer, in which DNA is transmitted from one bacterial host to another. RNA-binding that interacts with the traJ mRNA and its antisense RNA, finP, stabilizing finP against endonucleolytic degradation and facilitating sense-antisense RNA recognition (By similarity).
+[https://www.uniprot.org/uniprot/FINO3_ECOLX FINO3_ECOLX] One of the components on the FinOP fertility inhibition complex, which inhibits the expression of traJ gene, which in turn regulates the expression of some 20 transfer genes. The transfer genes are responsible for the process, called conjugal transfer, in which DNA is transmitted from one bacterial host to another. RNA-binding that interacts with the traJ mRNA and its antisense RNA, finP, stabilizing finP against endonucleolytic degradation and facilitating sense-antisense RNA recognition (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1dvo ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The conjugative transfer of F-like plasmids is repressed by FinO, an RNA binding protein. FinO interacts with the F-plasmid encoded traJ mRNA and its antisense RNA, FinP, stabilizing FinP against endonucleolytic degradation and facilitating sense-antisense RNA recognition. Here we present the 2.0 A resolution X-ray crystal structure of FinO, lacking its flexible N-terminal extension. FinO adopts a novel, elongated, largely helical conformation. An N-terminal region, previously shown to contact RNA, forms a positively charged alpha-helix (helix 1) that protrudes 45 A from the central core of FinO. A C-terminal region of FinO that is implicated in RNA interactions also extends out from the central body of the protein, adopting a helical conformation and packing against the base of the N-terminal helix. A highly positively charged patch on the surface of the FinO core may present another RNA binding surface. The results of an in vitro RNA duplexing assay demonstrate that the flexible N-terminal region of FinO plays a key role in FinP-traJ RNA recognition, and supports our proposal that this region and the N-terminus of helix 1 interact with and stabilize paired, complementary RNA loops in a kissing complex.
-Crystal structure of the bacterial conjugation repressor finO.,Ghetu AF, Gubbins MJ, Frost LS, Glover JN Nat Struct Biol. 2000 Jul;7(7):565-9. PMID:10876242<ref>PMID:10876242</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1dvo" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Frost, L S]]
+[[Category: Frost LS]]
-[[Category: Ghetu, A F]]
+[[Category: Ghetu AF]]
-[[Category: Glover, J N.M]]
+[[Category: Glover JNM]]
-[[Category: Gubbins, M J]]
+[[Category: Gubbins MJ]]
-[[Category: Bacterial conjugation]]
-[[Category: Repressor]]
-[[Category: Transcription]]