5j43
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==CdiA-CT from uropathogenic Escherichia coli in complex with CysK== | |
| - | + | <StructureSection load='5j43' size='340' side='right' caption='[[5j43]], [[Resolution|resolution]] 2.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5j43]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J43 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IT1:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>IT1</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5j5v|5j5v]], [[5j4a|5j4a]]</td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] </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=5j43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j43 OCA], [http://pdbe.org/5j43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j43 RCSB], [http://www.ebi.ac.uk/pdbsum/5j43 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j43 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CDIA_ECOL5 CDIA_ECOL5]] Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (target cell counts decrease 100- to 1000-fold). CdiA toxicity is neutralized by its cognate immunity protein CdiI, but not by CdiI from other bacteria (PubMed:23469034, PubMed:24889811). BamA on the target cells acts as a receptor for intact CdiA (PubMed:23469034). However isolated CdiA-CT is imported in an F-pilus-mediated fashion; CdiA-CT inhibits F-mediated conjugation, probably via its N-terminus (residues 3016-3097), although it is not clear if this is physiologically significant (PubMed:24889811). The C-terminal domain (CT) cleaves within tRNA anticodon loops (PubMed:22333533, PubMed:24889811); this activity is inhibited by cognate CdiI (PubMed:21085179, PubMed:22333533, PubMed:24889811). tRNase activity of CdiA-CT is stimulated by CysK, although the extreme C-terminus (residues 3098-3242) has tRNase activity in the absence of CysK. In vivo CDI toxicity requires CysK (PubMed:22333533, PubMed:24889811). Purified CdiA-CT (residues 3016-3242) inhibits E.coli cell growth when added to cultures alone or in complex with cognate CdiI, growth is inhibited when cognate CdiI is present within the cell but not when a CdiA-CT/CdiI complex is added extracellularly, suggesting CdiA-CT alone but not the CdiA-CT/CdiI complex is imported into the target cell (PubMed:24889811).<ref>PMID:21085179</ref> <ref>PMID:22333533</ref> <ref>PMID:23469034</ref> <ref>PMID:24889811</ref> <ref>PMID:25174572</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cysteine synthase]] | ||
| + | [[Category: Goulding, C W]] | ||
| + | [[Category: Johnson, P M]] | ||
| + | [[Category: Morse, R P]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Endonuclease]] | ||
| + | [[Category: Toxin]] | ||
Revision as of 15:44, 27 July 2016
CdiA-CT from uropathogenic Escherichia coli in complex with CysK
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