|
|
| Line 3: |
Line 3: |
| | <StructureSection load='3dor' size='340' side='right'caption='[[3dor]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='3dor' size='340' side='right'caption='[[3dor]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3dor]] 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=3DOR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3DOR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3dor]] 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=3DOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DOR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dja|3dja]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3dor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dor OCA], [http://pdbe.org/3dor PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dor RCSB], [http://www.ebi.ac.uk/pdbsum/3dor PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dor 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=3dor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dor OCA], [https://pdbe.org/3dor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dor RCSB], [https://www.ebi.ac.uk/pdbsum/3dor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dor ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Y858_CHLTR Y858_CHLTR] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 31: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Chlamydia trachomatis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chai, J]] | + | [[Category: Chai J]] |
| - | [[Category: Huang, Z]] | + | [[Category: Huang Z]] |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: Mature cpaf]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Y858_CHLTR
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The obligate intracellular pathogen Chlamydia trachomatis is the most common cause of sexually transmitted bacterial disease. It secretes a protease known as chlamydial protease/proteasome-like activity factor (CPAF) that degrades many host molecules and plays a major role in Chlamydia pathogenesis. Here, we show that mature CPAF is a homodimer of the catalytic domains, each of which comprises two distinct subunits. Dormancy of the CPAF zymogen is maintained by an internal inhibitory segment that binds the CPAF active site and blocks its homodimerization. CPAF activation is initiated by trans-autocatalytic cleavage, which induces homodimerization and conformational changes that assemble the catalytic triad. This assembly leads to two autocatalytic cleavages and removal of the inhibitory segment, enabling full CPAF activity. CPAF is covalently bound and inhibited by the proteasome inhibitor lactacystin. These results reveal the activation mechanism of the CPAF serine protease and suggest new opportunities for anti-Chlamydia drug development.
Structural basis for activation and inhibition of the secreted chlamydia protease CPAF.,Huang Z, Feng Y, Chen D, Wu X, Huang S, Wang X, Xiao X, Li W, Huang N, Gu L, Zhong G, Chai J Cell Host Microbe. 2008 Dec 11;4(6):529-42. PMID:19064254[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Huang Z, Feng Y, Chen D, Wu X, Huang S, Wang X, Xiao X, Li W, Huang N, Gu L, Zhong G, Chai J. Structural basis for activation and inhibition of the secreted chlamydia protease CPAF. Cell Host Microbe. 2008 Dec 11;4(6):529-42. PMID:19064254 doi:http://dx.doi.org/S1931-3128(08)00332-6
|
