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2l92

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[[Image:2l92.jpg|left|200px]]
 
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==Solution structure of the C-terminal domain of H-NS like protein Bv3F==
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The line below this paragraph, containing "STRUCTURE_2l92", creates the "Structure Box" on the page.
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<StructureSection load='2l92' size='340' side='right'caption='[[2l92]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2l92]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_vietnamiensis_G4 Burkholderia vietnamiensis G4]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L92 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2l92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l92 OCA], [https://pdbe.org/2l92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l92 RCSB], [https://www.ebi.ac.uk/pdbsum/2l92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l92 ProSAT]</span></td></tr>
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{{STRUCTURE_2l92| PDB=2l92 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BV3F_BURVG BV3F_BURVG] A DNA-binding protein implicated in transcriptional repression and chromosome organization and compaction. Binds in the minor groove of AT-rich DNA (PubMed:21673140). Binds nucleation sites in AT-rich DNA and bridges them, forming higher-order nucleoprotein complexes and condensing the chromosome. As many horizontally transferred genes are AT-rich, it plays a central role in silencing foreign genes (By similarity).[UniProtKB:P0ACF8]<ref>PMID:21673140</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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H-NS and Lsr2 are nucleoid-associated proteins from Gram-negative bacteria and Mycobacteria, respectively, that play an important role in the silencing of horizontally acquired foreign DNA that is more AT-rich than the resident genome. Despite the fact that Lsr2 and H-NS proteins are dissimilar in sequence and structure, they serve apparently similar functions and can functionally complement one another. The mechanism by which these xenogeneic silencers selectively target AT-rich DNA has been enigmatic. We performed high-resolution protein binding microarray analysis to simultaneously assess the binding preference of H-NS and Lsr2 for all possible 8-base sequences. Concurrently, we performed a detailed structure-function relationship analysis of their C-terminal DNA binding domains by NMR. Unexpectedly, we found that H-NS and Lsr2 use a common DNA binding mechanism where a short loop containing a "Q/RGR" motif selectively interacts with the DNA minor groove, where the highest affinity is for AT-rich sequences that lack A-tracts. Mutations of the Q/RGR motif abolished DNA binding activity. Netropsin, a DNA minor groove-binding molecule effectively outcompeted H-NS and Lsr2 for binding to AT-rich sequences. These results provide a unified molecular mechanism to explain findings related to xenogeneic silencing proteins, including their lack of apparent sequence specificity but preference for AT-rich sequences. Our findings also suggest that structural information contained within the DNA minor groove is deciphered by xenogeneic silencing proteins to distinguish genetic material that is self from nonself.
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===Solution structure of the C-terminal domain of H-NS like protein Bv3F===
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Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins.,Gordon BR, Li Y, Cote A, Weirauch MT, Ding P, Hughes TR, Navarre WW, Xia B, Liu J Proc Natl Acad Sci U S A. 2011 Jun 28;108(26):10690-5. Epub 2011 Jun 14. PMID:21673140<ref>PMID:21673140</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==About this Structure==
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</div>
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[[2l92]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_vietnamiensis Burkholderia vietnamiensis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L92 OCA].
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<div class="pdbe-citations 2l92" style="background-color:#fffaf0;"></div>
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[[Category: Burkholderia vietnamiensis]]
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== References ==
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[[Category: Li, Y.]]
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<references/>
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[[Category: Xia, B.]]
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__TOC__
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[[Category: At hook]]
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</StructureSection>
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[[Category: Dna binding protein]]
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[[Category: Burkholderia vietnamiensis G4]]
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[[Category: H-n]]
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[[Category: Large Structures]]
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[[Category: Li Y]]
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[[Category: Xia B]]

Current revision

Solution structure of the C-terminal domain of H-NS like protein Bv3F

PDB ID 2l92

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