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1rcw

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(New page: 200px<br /><applet load="1rcw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rcw, resolution 2.50&Aring;" /> '''Crystal structure of...)
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[[Image:1rcw.jpg|left|200px]]<br /><applet load="1rcw" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rcw, resolution 2.50&Aring;" />
 
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'''Crystal structure of CT610 from Chlamydia trachomatis'''<br />
 
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==Overview==
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==Crystal structure of CT610 from Chlamydia trachomatis==
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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.
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<StructureSection load='1rcw' size='340' side='right'caption='[[1rcw]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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1RCW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RCW OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<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>
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==Reference==
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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>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15087448 15087448]
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rc/1rcw_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Chlamydia trachomatis]]
[[Category: Chlamydia trachomatis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Liddington, R.C.]]
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[[Category: Liddington RC]]
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[[Category: Schwarzenbacher, R.]]
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[[Category: Schwarzenbacher R]]
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[[Category: FE]]
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[[Category: di-iron]]
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[[Category: iron]]
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[[Category: metallo enzyme]]
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[[Category: redox enzyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:28:43 2007''
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Current revision

Crystal structure of CT610 from Chlamydia trachomatis

PDB ID 1rcw

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