1rcw
From Proteopedia
(Difference between revisions)
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<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> | <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> | ||
</table> | </table> | ||
| - | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rc/1rcw_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rc/1rcw_consurf.spt"</scriptWhenChecked> | ||
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</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]. | </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> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| + | |||
| + | 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:15087448<ref>PMID:15087448</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1rcw" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of CT610 from Chlamydia trachomatis
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