4e1r

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e1r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E1R FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e1r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E1R FirstGlance]. <br>
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</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=4e1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1r OCA], [https://pdbe.org/4e1r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e1r RCSB], [https://www.ebi.ac.uk/pdbsum/4e1r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1r ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.041&#8491;</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=4e1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1r OCA], [https://pdbe.org/4e1r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e1r RCSB], [https://www.ebi.ac.uk/pdbsum/4e1r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1r ProSAT]</span></td></tr>
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== Function ==
== 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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[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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== Publication Abstract from PubMed ==
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Lsr2 is a small DNA-binding protein present in mycobacteria and related actinobacteria that regulates gene expression and influences the organization of bacterial chromatin. Lsr2 is a dimer that binds to AT-rich regions of chromosomal DNA and physically protects DNA from damage by reactive oxygen intermediates (ROI). A recent structure of the C-terminal DNA-binding domain of Lsr2 provides a rationale for its interaction with the minor groove of DNA, its preference for AT-rich tracts, and its similarity to other bacterial nucleoid-associated DNA-binding domains. In contrast, the details of Lsr2 dimerization (and oligomerization) via its N-terminal domain, and the mechanism of Lsr2-mediated chromosomal cross-linking and protection is unknown. We have solved the structure of the N-terminal domain of Lsr2 (N-Lsr2) at 1.73 A resolution using crystallographic ab initio approaches. The structure shows an intimate dimer of two ss-ss-a motifs with no close homologues in the structural databases. The organization of individual N-Lsr2 dimers in the crystal also reveals a mechanism for oligomerization. Proteolytic removal of three N-terminal residues from Lsr2 results in the formation of an anti-parallel beta-sheet between neighboring molecules and the formation of linear chains of N-Lsr2. Oligomerization can be artificially induced using low concentrations of trypsin and the arrangement of N-Lsr2 into long chains is observed in both monoclinic and hexagonal crystallographic space groups. In solution, oligomerization of N-Lsr2 is also observed following treatment with trypsin. A change in chromosomal topology after the addition of trypsin to full-length Lsr2-DNA complexes and protection of DNA towards DNAse digestion can be observed using electron microscopy and electrophoresis. These results suggest a mechanism for oligomerization of Lsr2 via protease-activation leading to chromosome compaction and protection, and concomitant down-regulation of large numbers of genes. This mechanism is likely to be relevant under conditions of stress where cellular proteases are known to be upregulated.
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The structure of the oligomerization domain of Lsr2 from Mycobacterium tuberculosis reveals a mechanism for chromosome organization and protection.,Summers EL, Meindl K, Uson I, Mitra AK, Radjainia M, Colangeli R, Alland D, Arcus VL PLoS One. 2012;7(6):e38542. doi: 10.1371/journal.pone.0038542. Epub 2012 Jun 13. PMID:22719899<ref>PMID:22719899</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 class="pdbe-citations 4e1r" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>

Current revision

Crystal structure of the dimerization domain of Lsr2 from Mycobacterium tuberculosis in the P 31 2 1 space group

PDB ID 4e1r

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