4e1p - Revision history

OCA at 11:01, 1 March 2024

2024-03-01T11:01:15Z

← Older revision		Revision as of 11:01, 1 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e1p]] 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=4E1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E1P FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e1p]] 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=4E1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E1P 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=4e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1p OCA], [https://pdbe.org/4e1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e1p RCSB], [https://www.ebi.ac.uk/pdbsum/4e1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1p 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]] 1.728Å</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=4e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1p OCA], [https://pdbe.org/4e1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e1p RCSB], [https://www.ebi.ac.uk/pdbsum/4e1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1p ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	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.

	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>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4e1p" style="background-color:#fffaf0;"></div~~>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:45, 28 September 2022

2022-09-28T06:45:13Z

← Older revision		Revision as of 06:45, 28 September 2022
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	==Crystal structure of the dimerization domain of Lsr2 from Mycobacterium tuberculosis in the P 1 21 1 space group==		==Crystal structure of the dimerization domain of Lsr2 from Mycobacterium tuberculosis in the P 1 21 1 space group==
	<StructureSection load='4e1p' size='340' side='right' caption='[[4e1p]], [[Resolution\|resolution]] 1.73Å' scene=''>		<StructureSection load='4e1p' size='340' side='right'caption='[[4e1p]], [[Resolution\|resolution]] 1.73Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e1p]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus~~ tuberculosis~~" (zopf 1883) klein 1884~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1P OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4E1P FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e1p]] 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=4E1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E1P FirstGlance]. <br>
	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e1r\|4e1r]]</td></tr>~~		</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=4e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1p OCA], [https://pdbe.org/4e1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e1p RCSB], [https://www.ebi.ac.uk/pdbsum/4e1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1p ProSAT]</span></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lsr2, MT3704, MTCY07H7B.25, Rv3597c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1p OCA], [~~http~~://pdbe.org/4e1p PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4e1p RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4e1p PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1p ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Arcus, V L~~]]		[[Category: Large Structures]]
	[[Category: ~~Meindl, K~~]]		[[Category: Mycobacterium tuberculosis]]
	[[Category: ~~Summers, E L~~]]		[[Category: Arcus VL]]
	[[Category: ~~Uson, I~~]]		[[Category: Meindl K]]
	[[Category: ~~Anti-parallel beta sheet~~]]		[[Category: Summers EL]]
	[[Category: ~~Dimer]]~~		[[Category: Uson I]]
	~~[[Category: Dna binding protein~~]]

OCA at 07:34, 5 August 2016

2016-08-05T07:34:19Z

← Older revision		Revision as of 07:34, 5 August 2016
Line 1:		Line 1:

	==Crystal structure of the dimerization domain of Lsr2 from Mycobacterium tuberculosis in the P 1 21 1 space group==		==Crystal structure of the dimerization domain of Lsr2 from Mycobacterium tuberculosis in the P 1 21 1 space group==
	<StructureSection load='4e1p' size='340' side='right' caption='[[4e1p]], [[Resolution\|resolution]] 1.73Å' scene=''>		<StructureSection load='4e1p' size='340' side='right' caption='[[4e1p]], [[Resolution\|resolution]] 1.73Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e1p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mycobacterium_tuberculosis Mycobacterium~~ tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E1P FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e1p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E1P FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e1r\|4e1r]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e1r\|4e1r]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lsr2, MT3704, MTCY07H7B.25, Rv3597c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 ~~Mycobacterium~~ tuberculosis])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lsr2, MT3704, MTCY07H7B.25, Rv3597c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e1p RCSB], [http://www.ebi.ac.uk/pdbsum/4e1p PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1p OCA], [http://pdbe.org/4e1p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e1p RCSB], [http://www.ebi.ac.uk/pdbsum/4e1p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1p ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 4e1p" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Mycobacterium tuberculosis]]~~
	[[Category: Arcus, V L]]		[[Category: Arcus, V L]]
	[[Category: Meindl, K]]		[[Category: Meindl, K]]

OCA at 00:19, 25 December 2014

2014-12-25T00:19:36Z

← Older revision		Revision as of 00:19, 25 December 2014
Line 7:		Line 7:
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e1p RCSB], [http://www.ebi.ac.uk/pdbsum/4e1p PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e1p RCSB], [http://www.ebi.ac.uk/pdbsum/4e1p PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 17:34, 9 December 2014

2014-12-09T17:34:53Z

← Older revision		Revision as of 17:34, 9 December 2014
Line 1:		Line 1:
	[[~~Image~~:~~4e1p~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal structure of the dimerization domain of Lsr2 from Mycobacterium tuberculosis in the P 1 21 1 space group==
			<StructureSection load='4e1p' size='340' side='right' caption='[[4e1p]], [[Resolution\|resolution]] 1.73Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4e1p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E1P FirstGlance]. <br>
			</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e1r\|4e1r]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lsr2, MT3704, MTCY07H7B.25, Rv3597c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</td></tr>
			<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e1p RCSB], [http://www.ebi.ac.uk/pdbsum/4e1p PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			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.

	~~{{STRUCTURE_4e1p\| PDB=4e1p \| SCENE= }}~~		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>

	~~===Crystal structure~~ of the ~~dimerization domain~~ of ~~Lsr2 from Mycobacterium tuberculosis in the P 1 21 1 space group===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_22719899}}~~		== References ==
			<references/>
	==~~About this Structure~~==		__TOC__
	~~[[4e1p]] is a 2 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1P OCA].~~		</StructureSection>
	[[Category: Mycobacterium tuberculosis]]		[[Category: Mycobacterium tuberculosis]]
	[[Category: Arcus, V L.]]		[[Category: Arcus, V L]]
	[[Category: Meindl, K.]]		[[Category: Meindl, K]]
	[[Category: Summers, E L.]]		[[Category: Summers, E L]]
	[[Category: Uson, I.]]		[[Category: Uson, I]]
	[[Category: Anti-parallel beta sheet]]		[[Category: Anti-parallel beta sheet]]
	[[Category: Dimer]]		[[Category: Dimer]]
	[[Category: Dna binding protein]]		[[Category: Dna binding protein]]

OCA at 11:41, 23 January 2013

2013-01-23T11:41:33Z

← Older revision		Revision as of 11:41, 23 January 2013
Line 1:		Line 1:
	[[Image:4e1p.~~jpg~~\|left\|200px]]		[[Image:4e1p.png\|left\|200px]]

	{{STRUCTURE_4e1p\| PDB=4e1p \| SCENE= }}		{{STRUCTURE_4e1p\| PDB=4e1p \| SCENE= }}
Line 5:		Line 5:
	===Crystal structure of the dimerization domain of Lsr2 from Mycobacterium tuberculosis in the P 1 21 1 space group===		===Crystal structure of the dimerization domain of Lsr2 from Mycobacterium tuberculosis in the P 1 21 1 space group===

			{{ABSTRACT_PUBMED_22719899}}

	==About this Structure==		==About this Structure==

OCA at 07:58, 20 June 2012

2012-06-20T07:58:12Z

← Older revision		Revision as of 07:58, 20 June 2012
Line 1:		Line 1:
	~~'''Unreleased structure'''~~		[[Image:4e1p.jpg\|left\|200px]]

	~~The entry~~ 4e1p ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4e1p\| PDB=4e1p \| SCENE= }}

	~~Authors: Summers, E.L., Meindl, K., Uson, I., Arcus, V.L.~~		===Crystal structure of the dimerization domain of Lsr2 from Mycobacterium tuberculosis in the P 1 21 1 space group===

	~~Description~~: ~~Crystal structure of the dimerization domain of Lsr2~~ from Mycobacterium tuberculosis ~~in the P 1 21 1 space group~~
			==About this Structure==
			[[4e1p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1P OCA].
			[[Category: Mycobacterium tuberculosis]]
			[[Category: Arcus, V L.]]
			[[Category: Meindl, K.]]
			[[Category: Summers, E L.]]
			[[Category: Uson, I.]]
			[[Category: Anti-parallel beta sheet]]
			[[Category: Dimer]]
			[[Category: Dna binding protein]]

OCA at 18:53, 2 May 2012

2012-05-02T18:53:05Z

← Older revision		Revision as of 18:53, 2 May 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4e1p is ON HOLD		The entry 4e1p is ON HOLD until Paper Publication

	Authors: Summers, E.L., Meindl, K., Uson, I., Arcus, V.L.		Authors: Summers, E.L., Meindl, K., Uson, I., Arcus, V.L.

	Description: Crystal structure of dimerization domain of Lsr2 from Mycobacterium tuberculosis		Description: Crystal structure of the dimerization domain of Lsr2 from Mycobacterium tuberculosis in the P 1 21 1 space group

OCA at 07:14, 21 March 2012

2012-03-21T07:14:39Z

← Older revision		Revision as of 07:14, 21 March 2012
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	Authors: Summers, E.L., Meindl, K., Uson, I., Arcus, V.L.		Authors: Summers, E.L., Meindl, K., Uson, I., Arcus, V.L.

	Description: Crystal structure of ~~dimerisation~~ domain of Lsr2 from Mycobacterium tuberculosis		Description: Crystal structure of dimerization domain of Lsr2 from Mycobacterium tuberculosis

OCA: Protected "4e1p" [edit=sysop:move=sysop]

2012-03-14T06:16:15Z

Protected "4e1p" [edit=sysop:move=sysop]

← Older revision	Revision as of 06:16, 14 March 2012
(No difference)