3qyx

From Proteopedia

(Difference between revisions)

Revision as of 05:41, 15 June 2022

Crystal structure of Mycobacterium tuberculosis EspR in complex with a small DNA fragment

Structural highlights

3qyx is a 5 chain structure with sequence from Myctu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3qf3, 3qwg
Gene:	espR, MT3964, Rv3849 (MYCTU)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ESPR_MYCTU] Virulence regulator that has both architectural and regulatory roles. Impacts cell wall functions and pathogenesis through regulation of multiple genes, including the espACD operon, which is a key ESX-1 component. Influences target gene expression positively or negatively, depending on its binding position relative to the genes it controls. Acts by binding directly to the DNA. May play a central role in regulating virulence gene expression.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

The human pathogen Mycobacterium tuberculosis requires the ESX-1 secretion system for full virulence. EspR plays a key role in ESX-1 regulation via direct binding and transcriptional activation of the espACD operon. Here, we describe the crystal structures of EspR, a C-terminally truncated form, EspRDelta10, as well as an EspR-DNA complex. EspR forms a dimer with each monomer containing an N-terminal helix-turn-helix DNA binding motif and an atypical C-terminal dimerization domain. Structural studies combined with footprinting experiments, atomic force microscopy and molecular dynamic simulations allow us to propose a model in which a dimer of EspR dimers is the minimal functional unit with two subunits binding two consecutive major grooves. The other two DNA binding domains are thus free to form higher-order oligomers and to bridge distant DNA sites in a cooperative way. These features are reminiscent of nucleoid-associated proteins and suggest a more general regulatory role for EspR than was previously suspected.

Atypical DNA recognition mechanism used by the EspR virulence regulator of Mycobacterium tuberculosis.,Blasco B, Stenta M, Alonso-Sarduy L, Dietler G, Peraro MD, Cole ST, Pojer F Mol Microbiol. 2011 Aug 30. doi: 10.1111/j.1365-2958.2011.07813.x. PMID:21883526^[5]

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

References

↑ Raghavan S, Manzanillo P, Chan K, Dovey C, Cox JS. Secreted transcription factor controls Mycobacterium tuberculosis virulence. Nature. 2008 Aug 7;454(7205):717-21. doi: 10.1038/nature07219. PMID:18685700 doi:http://dx.doi.org/10.1038/nature07219
↑ Hunt DM, Sweeney NP, Mori L, Whalan RH, Comas I, Norman L, Cortes T, Arnvig KB, Davis EO, Stapleton MR, Green J, Buxton RS. Long-range transcriptional control of an operon necessary for virulence-critical ESX-1 secretion in Mycobacterium tuberculosis. J Bacteriol. 2012 May;194(9):2307-20. doi: 10.1128/JB.00142-12. Epub 2012 Mar 2. PMID:22389481 doi:http://dx.doi.org/10.1128/JB.00142-12
↑ Blasco B, Chen JM, Hartkoorn R, Sala C, Uplekar S, Rougemont J, Pojer F, Cole ST. Virulence regulator EspR of Mycobacterium tuberculosis is a nucleoid-associated protein. PLoS Pathog. 2012;8(3):e1002621. doi: 10.1371/journal.ppat.1002621. Epub 2012 Mar, 29. PMID:22479184 doi:http://dx.doi.org/10.1371/journal.ppat.1002621
↑ Blasco B, Stenta M, Alonso-Sarduy L, Dietler G, Peraro MD, Cole ST, Pojer F. Atypical DNA recognition mechanism used by the EspR virulence regulator of Mycobacterium tuberculosis. Mol Microbiol. 2011 Aug 30. doi: 10.1111/j.1365-2958.2011.07813.x. PMID:21883526 doi:10.1111/j.1365-2958.2011.07813.x
↑ Blasco B, Stenta M, Alonso-Sarduy L, Dietler G, Peraro MD, Cole ST, Pojer F. Atypical DNA recognition mechanism used by the EspR virulence regulator of Mycobacterium tuberculosis. Mol Microbiol. 2011 Aug 30. doi: 10.1111/j.1365-2958.2011.07813.x. PMID:21883526 doi:10.1111/j.1365-2958.2011.07813.x

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3qyx"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Mycobacterium tuberculosis EspR in complex with a small DNA fragment==
-<StructureSection load='3qyx' size='340' side='right' caption='[[3qyx]], [[Resolution|resolution]] 3.75&Aring;' scene=''>
+<StructureSection load='3qyx' size='340' side='right'caption='[[3qyx]], [[Resolution|resolution]] 3.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3qyx]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QYX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3qyx]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QYX FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qf3|3qf3]], [[3qwg|3qwg]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qf3|3qf3]], [[3qwg|3qwg]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">espR, MT3964, Rv3849 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">espR, MT3964, Rv3849 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=3qyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qyx OCA], [http://pdbe.org/3qyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qyx RCSB], [http://www.ebi.ac.uk/pdbsum/3qyx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qyx ProSAT]</span></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=3qyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qyx OCA], [https://pdbe.org/3qyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qyx RCSB], [https://www.ebi.ac.uk/pdbsum/3qyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qyx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ESPR_MYCTU ESPR_MYCTU]] Virulence regulator that has both architectural and regulatory roles. Impacts cell wall functions and pathogenesis through regulation of multiple genes, including the espACD operon, which is a key ESX-1 component. Influences target gene expression positively or negatively, depending on its binding position relative to the genes it controls. Acts by binding directly to the DNA. May play a central role in regulating virulence gene expression.<ref>PMID:18685700</ref> <ref>PMID:22389481</ref> <ref>PMID:22479184</ref> <ref>PMID:21883526</ref>
+[[https://www.uniprot.org/uniprot/ESPR_MYCTU ESPR_MYCTU]] Virulence regulator that has both architectural and regulatory roles. Impacts cell wall functions and pathogenesis through regulation of multiple genes, including the espACD operon, which is a key ESX-1 component. Influences target gene expression positively or negatively, depending on its binding position relative to the genes it controls. Acts by binding directly to the DNA. May play a central role in regulating virulence gene expression.<ref>PMID:18685700</ref> <ref>PMID:22389481</ref> <ref>PMID:22479184</ref> <ref>PMID:21883526</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Myctu]]
 [[Category: Blasco, B]]

3qyx

From Proteopedia

Revision as of 05:41, 15 June 2022

Crystal structure of Mycobacterium tuberculosis EspR in complex with a small DNA fragment

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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