5b5q
From Proteopedia
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<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. 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 [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> |
</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"><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'>[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> | <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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:28347402</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5b5q" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 09:46, 22 November 2017
1.7 Angstroms structure of ChlaDub1 from Chlamydia Trachomatis
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