2kng

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of C-domain of Lsr2

Structural highlights

2kng is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[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

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.

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Colangeli R, Helb D, Vilcheze C, Hazbon MH, Lee CG, Safi H, Sayers B, Sardone I, Jones MB, Fleischmann RD, Peterson SN, Jacobs WR Jr, Alland D. Transcriptional regulation of multi-drug tolerance and antibiotic-induced responses by the histone-like protein Lsr2 in M. tuberculosis. PLoS Pathog. 2007 Jun;3(6):e87. PMID:17590082 doi:http://dx.doi.org/10.1371/journal.ppat.0030087
↑ Chen JM, Ren H, Shaw JE, Wang YJ, Li M, Leung AS, Tran V, Berbenetz NM, Kocincova D, Yip CM, Reyrat JM, Liu J. Lsr2 of Mycobacterium tuberculosis is a DNA-bridging protein. Nucleic Acids Res. 2008 Apr;36(7):2123-35. doi: 10.1093/nar/gkm1162. Epub 2008, Jan 10. PMID:18187505 doi:http://dx.doi.org/10.1093/nar/gkm1162
↑ Colangeli R, Haq A, Arcus VL, Summers E, Magliozzo RS, McBride A, Mitra AK, Radjainia M, Khajo A, Jacobs WR Jr, Salgame P, Alland D. The multifunctional histone-like protein Lsr2 protects mycobacteria against reactive oxygen intermediates. Proc Natl Acad Sci U S A. 2009 Mar 17;106(11):4414-8. doi:, 10.1073/pnas.0810126106. Epub 2009 Feb 23. PMID:19237572 doi:http://dx.doi.org/10.1073/pnas.0810126106
↑ Gordon BR, Li Y, Wang L, Sintsova A, van Bakel H, Tian S, Navarre WW, Xia B, Liu J. Lsr2 is a nucleoid-associated protein that targets AT-rich sequences and virulence genes in Mycobacterium tuberculosis. Proc Natl Acad Sci U S A. 2010 Jan 20. PMID:20133735
↑ Gordon BR, Li Y, Wang L, Sintsova A, van Bakel H, Tian S, Navarre WW, Xia B, Liu J. Lsr2 is a nucleoid-associated protein that targets AT-rich sequences and virulence genes in Mycobacterium tuberculosis. Proc Natl Acad Sci U S A. 2010 Jan 20. PMID:20133735

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2kng"

Categories: Large Structures | Mycobacterium tuberculosis | Li Y | Xia B

@@ Line 1: / Line 1: @@
 ==Solution structure of C-domain of Lsr2==
-<StructureSection load='2kng' size='340' side='right'caption='[[2kng]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2kng' size='340' side='right'caption='[[2kng]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2kng]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. 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>
+<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>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lsr2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
+</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=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>
 </table>
 == Function ==
-[[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>
+[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Li, Y]]
+[[Category: Mycobacterium tuberculosis]]
-[[Category: Xia, B]]
+[[Category: Li Y]]
-[[Category: Dna binding protein]]
+[[Category: Xia B]]
-[[Category: Dna-binding domain]]
-[[Category: Immune response]]

2kng

From Proteopedia

Current revision

Solution structure of C-domain of Lsr2

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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