2kng

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{{Seed}}
 
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[[Image:2kng.jpg|left|200px]]
 
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==Solution structure of C-domain of Lsr2==
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The line below this paragraph, containing "STRUCTURE_2kng", creates the "Structure Box" on the page.
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<StructureSection load='2kng' size='340' side='right'caption='[[2kng]]' 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'>[[2kng]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KNG FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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=2kng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kng OCA], [https://pdbe.org/2kng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kng RCSB], [https://www.ebi.ac.uk/pdbsum/2kng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kng ProSAT]</span></td></tr>
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{{STRUCTURE_2kng| PDB=2kng | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LSR2_MYCTU LSR2_MYCTU] DNA-bridging protein that has both architectural and regulatory roles. Influences the organization of chromatin and gene expression by binding non-specifically to DNA, with a preference for AT-rich sequences, and bridging distant DNA segments. Represses expression of multiple genes involved in a broad range of cellular processes, including major virulence factors or antibiotic-induced genes, such as iniBAC or efpA. May coordinate global gene regulation and virulence. Also protects mycobacteria against reactive oxygen intermediates during macrophage infection by acting as a physical barrier to DNA degradation.<ref>PMID:17590082</ref> <ref>PMID:18187505</ref> <ref>PMID:19237572</ref> <ref>PMID:20133735</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kn/2kng_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2kng ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bacterial nucleoid-associated proteins play important roles in chromosome organization and global gene regulation. We find that Lsr2 of Mycobacterium tuberculosis is a unique nucleoid-associated protein that binds AT-rich regions of the genome, including genomic islands acquired by horizontal gene transfer and regions encoding major virulence factors, such as the ESX secretion systems, the lipid virulence factors PDIM and PGL, and the PE/PPE families of antigenic proteins. Comparison of genome-wide binding data with expression data indicates that Lsr2 binding results in transcriptional repression. Domain-swapping experiments demonstrate that Lsr2 has an N-terminal dimerization domain and a C-terminal DNA-binding domain. Nuclear magnetic resonance analysis of the DNA-binding domain of Lsr2 and its interaction with DNA reveals a unique structure and a unique mechanism that enables Lsr2 to discriminately target AT-rich sequences through interactions with the minor groove of DNA. Taken together, we provide evidence that mycobacteria have employed a structurally distinct molecule with an apparently different DNA recognition mechanism to achieve a function similar to the Enterobacteriaceae H-NS, likely coordinating global gene regulation and virulence in this group of medically important bacteria.
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===Solution structure of C-domain of Lsr2===
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Lsr2 is a nucleoid-associated protein that targets AT-rich sequences and virulence genes in Mycobacterium tuberculosis.,Gordon BR, Li Y, Wang L, Sintsova A, van Bakel H, Tian S, Navarre WW, Xia B, Liu J Proc Natl Acad Sci U S A. 2010 Jan 20. PMID:20133735<ref>PMID:20133735</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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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20133735}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2kng" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20133735 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20133735}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2KNG is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KNG OCA].
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==Reference==
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<ref group="xtra">PMID:20133735</ref><references group="xtra"/>
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Li, Y.]]
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[[Category: Li Y]]
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[[Category: Xia, B.]]
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[[Category: Xia B]]
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[[Category: Dna binding protein]]
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[[Category: Dna-binding domain]]
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[[Category: Immune response]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 17 09:33:44 2010''
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Current revision

Solution structure of C-domain of Lsr2

PDB ID 2kng

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