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| | ==1.7 Angstroms structure of ChlaDub1 from Chlamydia Trachomatis== | | ==1.7 Angstroms structure of ChlaDub1 from Chlamydia Trachomatis== |
| - | <StructureSection load='5b5q' size='340' side='right' caption='[[5b5q]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='5b5q' size='340' side='right'caption='[[5b5q]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5b5q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"chlamydozoon_trachomatis"_(busacca_1935)_moshkovski_1945 "chlamydozoon trachomatis" (busacca 1935) moshkovski 1945]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B5Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B5Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5b5q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B5Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B5Q FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cdu1, ERS066953_00737 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=813 "Chlamydozoon trachomatis" (Busacca 1935) Moshkovski 1945]), CT868 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=813 "Chlamydozoon trachomatis" (Busacca 1935) Moshkovski 1945])</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=5b5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b5q OCA], [https://pdbe.org/5b5q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b5q RCSB], [https://www.ebi.ac.uk/pdbsum/5b5q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b5q 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=5b5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b5q OCA], [http://pdbe.org/5b5q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b5q RCSB], [http://www.ebi.ac.uk/pdbsum/5b5q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b5q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CDUB1_CHLT2 CDUB1_CHLT2] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protease possesses deubiquitinating and deneddylating activities (By similarity). Impairs ubiquitination and degradation of NF-kappa-B inhibitor alpha (NFKBIA), thereby preventing NF-kappa-B activation.<ref>PMID:18503636</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: Kisker, C]] | + | [[Category: Chlamydia trachomatis]] |
| - | [[Category: Ramirez, Y A]] | + | [[Category: Large Structures]] |
| - | [[Category: Sauer, F]] | + | [[Category: Kisker C]] |
| - | [[Category: Chlamydia trachomati]] | + | [[Category: Ramirez YA]] |
| - | [[Category: Deubiquitinase]] | + | [[Category: Sauer F]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
CDUB1_CHLT2 Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protease possesses deubiquitinating and deneddylating activities (By similarity). Impairs ubiquitination and degradation of NF-kappa-B inhibitor alpha (NFKBIA), thereby preventing NF-kappa-B activation.[1]
Publication Abstract from PubMed
Obligate intracellular Chlamydia trachomatis replicate in a membrane-bound vacuole called inclusion, which serves as a signaling interface with the host cell. Here, we show that the chlamydial deubiquitinating enzyme (Cdu) 1 localizes in the inclusion membrane and faces the cytosol with the active deubiquitinating enzyme domain. The structure of this domain revealed high similarity to mammalian deubiquitinases with a unique alpha-helix close to the substrate-binding pocket. We identified the apoptosis regulator Mcl-1 as a target that interacts with Cdu1 and is stabilized by deubiquitination at the chlamydial inclusion. A chlamydial transposon insertion mutant in the Cdu1-encoding gene exhibited increased Mcl-1 and inclusion ubiquitination and reduced Mcl-1 stabilization. Additionally, inactivation of Cdu1 led to increased sensitivity of C. trachomatis for IFNgamma and impaired infection in mice. Thus, the chlamydial inclusion serves as an enriched site for a deubiquitinating activity exerting a function in selective stabilization of host proteins and protection from host defense.
Chlamydia trachomatis-containing vacuole serves as deubiquitination platform to stabilize Mcl-1 and to interfere with host defense.,Fischer A, Harrison KS, Ramirez Y, Auer D, Chowdhury SR, Prusty BK, Sauer F, Dimond Z, Kisker C, Scott Hefty P, Rudel T Elife. 2017 Mar 28;6. pii: e21465. doi: 10.7554/eLife.21465. PMID:28347402[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Le Negrate G, Krieg A, Faustin B, Loeffler M, Godzik A, Krajewski S, Reed JC. ChlaDub1 of Chlamydia trachomatis suppresses NF-kappaB activation and inhibits IkappaBalpha ubiquitination and degradation. Cell Microbiol. 2008 Sep;10(9):1879-92. doi: 10.1111/j.1462-5822.2008.01178.x., Epub 2008 Jun 28. PMID:18503636 doi:http://dx.doi.org/10.1111/j.1462-5822.2008.01178.x
- ↑ Fischer A, Harrison KS, Ramirez Y, Auer D, Chowdhury SR, Prusty BK, Sauer F, Dimond Z, Kisker C, Scott Hefty P, Rudel T. Chlamydia trachomatis-containing vacuole serves as deubiquitination platform to stabilize Mcl-1 and to interfere with host defense. Elife. 2017 Mar 28;6. pii: e21465. doi: 10.7554/eLife.21465. PMID:28347402 doi:http://dx.doi.org/10.7554/eLife.21465
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