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| | ==Crystal STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ESX-1 SECRETED PROTEIN REGULATOR (EspR)== | | ==Crystal STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ESX-1 SECRETED PROTEIN REGULATOR (EspR)== |
| - | <StructureSection load='4ndw' size='340' side='right' caption='[[4ndw]], [[Resolution|resolution]] 3.30Å' scene=''> | + | <StructureSection load='4ndw' size='340' side='right'caption='[[4ndw]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ndw]] 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=4NDW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NDW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ndw]] 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=4NDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NDW FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qf3|3qf3]], [[3r1f|3r1f]]</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]] 3.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">espR, MT3964, Rv3849, RV3849C ([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'>[https://proteopedia.org/fgij/fg.htm?mol=4ndw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ndw OCA], [https://pdbe.org/4ndw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ndw RCSB], [https://www.ebi.ac.uk/pdbsum/4ndw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ndw ProSAT]</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=4ndw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ndw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ndw RCSB], [http://www.ebi.ac.uk/pdbsum/4ndw PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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;">
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| - | == Publication Abstract from PubMed ==
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| - | The Mycobacterium tuberculosis ESX-1 secreted protein regulator (EspR, Rv3849) is the key protein that delivers bacterial proteins into the host cell during mycobacterial infection. EspR binds directly to the espACD operon and is involved in transcriptional activation. In the current study, M. tuberculosis EspR has been crystallized and its X-ray structure has been determined at 3.3 A resolution in a P3221 crystal form. EspR forms a physiological dimer in the crystal. Each EspR monomer contains an N-terminal helix-turn-helix DNA-binding domain and a C-terminal dimerization domain. The EspR structure in the P3221 crystal form was compared with previously determined EspR structures in P32, P21 and P212121 crystal forms. Structural comparison analysis indicated that the N-terminal helix-turn-helix domain of EspR acquires a rigid structure in the four crystal forms. However, significant structural differences were observed in the C-terminal domain of EspR in the P21 crystal form when compared with the P3221 and P32 crystal forms. The interaction, stabilization energy and buried surface area analysis of EspR in the four different crystal forms have provided information about the physiological dimer interface of EspR.
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| - | Comparison of four different crystal forms of the Mycobacterium tuberculosis ESX-1 secreted protein regulator EspR.,Gangwar SP, Meena SR, Saxena AK Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):433-7. doi:, 10.1107/S2053230X14004166. Epub 2014 Mar 25. PMID:24699733<ref>PMID:24699733</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Gangwar, S P]] | + | [[Category: Large Structures]] |
| - | [[Category: Meena, S R]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Saxena, A K]] | + | [[Category: Gangwar SP]] |
| - | [[Category: All helical]] | + | [[Category: Meena SR]] |
| - | [[Category: Dna binding]] | + | [[Category: Saxena AK]] |
| - | [[Category: Helix-turn-helix motif]]
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| - | [[Category: Transactional regulator]]
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| - | [[Category: Transcription]]
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| Structural highlights
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]
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
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