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| - | [[Image:1rcw.jpg|left|200px]] | |
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| - | {{Structure
| + | ==Crystal structure of CT610 from Chlamydia trachomatis== |
| - | |PDB= 1rcw |SIZE=350|CAPTION= <scene name='initialview01'>1rcw</scene>, resolution 2.50Å
| + | <StructureSection load='1rcw' size='340' side='right'caption='[[1rcw]], [[Resolution|resolution]] 2.50Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> | + | <table><tr><td colspan='2'>[[1rcw]] is a 3 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=1RCW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RCW FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | |GENE= CT610 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=813 Chlamydia trachomatis])
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rcw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rcw OCA], [https://pdbe.org/1rcw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rcw RCSB], [https://www.ebi.ac.uk/pdbsum/1rcw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rcw ProSAT]</span></td></tr> |
| - | |RELATEDENTRY=
| + | </table> |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rcw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rcw OCA], [http://www.ebi.ac.uk/pdbsum/1rcw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rcw RCSB]</span>
| + | == Function == |
| - | }}
| + | [https://www.uniprot.org/uniprot/CADD_CHLTR CADD_CHLTR] Involved in de novo para-aminobenzoate (PABA) biosynthesis (PubMed:23972426, PubMed:32967910, PubMed:36122239). Acts as a self-sacrificing or 'suicide' enzyme that utilizes its own active site tyrosine residue(s) as the substrate for PABA synthesis (PubMed:32967910, PubMed:36122239). The side chain of the tyrosine residue is released from the protein backbone via cleavage of the C(alpha)-C(beta) bond, leaving a glycine in place of the original tyrosine residue (PubMed:32967910, PubMed:36122239). Reaction requires O(2) and a reduced dimetal cofactor (PubMed:32967910, PubMed:36122239).<ref>PMID:23972426</ref> <ref>PMID:32967910</ref> <ref>PMID:36122239</ref> Was also identified as a specific toxin that associates with death domains of tumor necrosis factor family (TNF) receptors and induces apoptosis in mammalian cell lines through a Caspase-dependent mechanism.<ref>PMID:11805081</ref> <ref>PMID:15087448</ref> |
| - | | + | == Evolutionary Conservation == |
| - | '''Crystal structure of CT610 from Chlamydia trachomatis'''
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | | + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | ==Overview== | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rc/1rcw_consurf.spt"</scriptWhenChecked> |
| - | The Chlamydia protein CADD (Chlamydia protein associating with death domains) has been implicated in the modulation of host cell apoptosis via binding to the death domains of tumor necrosis factor family receptors. Transfection of CADD into mammalian cells induces apoptosis. Here we present the CADD crystal structure, which reveals a dimer of seven-helix bundles. Each bundle contains a di-iron center adjacent to an internal cavity, forming an active site similar to that of methane mono-oxygenase hydrolase. We further show that CADD mutants lacking critical metal-coordinating residues are substantially less effective in inducing apoptosis but retain their ability to bind to death domains. We conclude that CADD is a novel redox protein toxin unique to Chlamydia species and propose that both its redox activity and death domain binding ability are required for its biological activity. | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | ==About this Structure== | + | </jmolCheckbox> |
| - | 1RCW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RCW OCA].
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rcw ConSurf]. |
| - | | + | <div style="clear:both"></div> |
| - | ==Reference== | + | == References == |
| - | Structure of the Chlamydia protein CADD reveals a redox enzyme that modulates host cell apoptosis., Schwarzenbacher R, Stenner-Liewen F, Liewen H, Robinson H, Yuan H, Bossy-Wetzel E, Reed JC, Liddington RC, J Biol Chem. 2004 Jul 9;279(28):29320-4. Epub 2004 Apr 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15087448 15087448]
| + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | [[Category: Chlamydia trachomatis]] | | [[Category: Chlamydia trachomatis]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Liddington, R C.]] | + | [[Category: Liddington RC]] |
| - | [[Category: Schwarzenbacher, R.]] | + | [[Category: Schwarzenbacher R]] |
| - | [[Category: di-iron]]
| + | |
| - | [[Category: iron]]
| + | |
| - | [[Category: metallo enzyme]]
| + | |
| - | [[Category: redox enzyme]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:26:22 2008''
| + | |
| Structural highlights
Function
CADD_CHLTR Involved in de novo para-aminobenzoate (PABA) biosynthesis (PubMed:23972426, PubMed:32967910, PubMed:36122239). Acts as a self-sacrificing or 'suicide' enzyme that utilizes its own active site tyrosine residue(s) as the substrate for PABA synthesis (PubMed:32967910, PubMed:36122239). The side chain of the tyrosine residue is released from the protein backbone via cleavage of the C(alpha)-C(beta) bond, leaving a glycine in place of the original tyrosine residue (PubMed:32967910, PubMed:36122239). Reaction requires O(2) and a reduced dimetal cofactor (PubMed:32967910, PubMed:36122239).[1] [2] [3] Was also identified as a specific toxin that associates with death domains of tumor necrosis factor family (TNF) receptors and induces apoptosis in mammalian cell lines through a Caspase-dependent mechanism.[4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Satoh Y, Kuratsu M, Kobayashi D, Dairi T. New gene responsible for para-aminobenzoate biosynthesis. J Biosci Bioeng. 2014 Feb;117(2):178-183. PMID:23972426 doi:10.1016/j.jbiosc.2013.07.013
- ↑ Macias-Orihuela Y, Cast T, Crawford I, Brandecker KJ, Thiaville JJ, Murzin AG, de Crécy-Lagard V, White RH, Allen KD. An Unusual Route for p-Aminobenzoate Biosynthesis in Chlamydia trachomatis Involves a Probable Self-Sacrificing Diiron Oxygenase. J Bacteriol. 2020 Sep 23;202(20):e00319-20. PMID:32967910 doi:10.1128/JB.00319-20
- ↑ Manley OM, Phan HN, Stewart AK, Mosley DA, Xue S, Cha L, Bai H, Lightfoot VC, Rucker PA, Collins L, Williams TI, Chang WC, Guo Y, Makris TM. Self-sacrificial tyrosine cleavage by an Fe:Mn oxygenase for the biosynthesis of para-aminobenzoate in Chlamydia trachomatis. Proc Natl Acad Sci U S A. 2022 Sep 27;119(39):e2210908119. PMID:36122239 doi:10.1073/pnas.2210908119
- ↑ Stenner-Liewen F, Liewen H, Zapata JM, Pawlowski K, Godzik A, Reed JC. CADD, a Chlamydia protein that interacts with death receptors. J Biol Chem. 2002 Mar 22;277(12):9633-6. PMID:11805081 doi:10.1074/jbc.C100693200
- ↑ Schwarzenbacher R, Stenner-Liewen F, Liewen H, Robinson H, Yuan H, Bossy-Wetzel E, Reed JC, Liddington RC. Structure of the Chlamydia protein CADD reveals a redox enzyme that modulates host cell apoptosis. J Biol Chem. 2004 Jul 9;279(28):29320-4. Epub 2004 Apr 15. PMID:15087448 doi:10.1074/jbc.M401268200
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