1tfk

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[[Image:1tfk.gif|left|200px]]
 
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{{Structure
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==Ribonuclease from Escherichia coli complexed with its inhibtor protein==
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|PDB= 1tfk |SIZE=350|CAPTION= <scene name='initialview01'>1tfk</scene>, resolution 2.10&Aring;
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<StructureSection load='1tfk' size='340' side='right'caption='[[1tfk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>
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<table><tr><td colspan='2'>[[1tfk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TFK FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.1&#8491;</td></tr>
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|GENE= CDA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), CDI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
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|DOMAIN=
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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=1tfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tfk OCA], [https://pdbe.org/1tfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tfk RCSB], [https://www.ebi.ac.uk/pdbsum/1tfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tfk ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1tfo|1TFO]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tfk OCA], [http://www.ebi.ac.uk/pdbsum/1tfk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tfk RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/CEAD_ECOLX CEAD_ECOLX] Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria. Colicin D inhibits protein synthesis.
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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/tf/1tfk_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=1tfk ConSurf].
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<div style="clear:both"></div>
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'''Ribonuclease from Escherichia coli complexed with its inhibtor protein'''
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==See Also==
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*[[Colicin 3D structures|Colicin 3D structures]]
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*[[Colicin immunity protein 3D structures|Colicin immunity protein 3D structures]]
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==Overview==
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__TOC__
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Colicin D is a plasmid-encoded proteinaceous toxin which kills sensitive Escherichia coli. Toxicity stems from ribonuclease activity that targets exclusively four isoacceptors of tRNA(Arg) with a cleavage position between 38 and 39 of the corresponding anticodons. Since no other tRNAs with the same sequences at 38 and 39 as tRNA(Arg)s are cleaved, colicin D should be capable of recognizing some higher order structure of tRNAs. We report here two crystal structures of catalytic domains of colicin D which have different N-terminal lengths, both complexed with its cognate inhibitor protein, ImmD. A row of positive charge patches is found on the surface of the catalytic domain, suggestive of the binding site of the tRNAs. This finding, together with our refined tRNase activity experiments, indicates that the catalytic domain starting at position 595 has activity almost equivalent to that of colicin D.
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</StructureSection>
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==About this Structure==
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1TFK is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFK OCA].
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==Reference==
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Relation between tRNase activity and the structure of colicin D according to X-ray crystallography., Yajima S, Nakanishi K, Takahashi K, Ogawa T, Hidaka M, Kezuka Y, Nonaka T, Ohsawa K, Masaki H, Biochem Biophys Res Commun. 2004 Sep 24;322(3):966-73. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15336558 15336558]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Hidaka, M.]]
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[[Category: Hidaka M]]
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[[Category: Kezuka, Y.]]
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[[Category: Kezuka Y]]
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[[Category: Masaki, H.]]
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[[Category: Masaki H]]
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[[Category: Nakanishi, K.]]
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[[Category: Nakanishi K]]
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[[Category: Nonaka, T.]]
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[[Category: Nonaka T]]
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[[Category: Ogawa, T.]]
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[[Category: Ogawa T]]
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[[Category: Ohsawa, K.]]
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[[Category: Ohsawa K]]
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[[Category: Takahashi, K.]]
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[[Category: Takahashi K]]
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[[Category: Yajima, S.]]
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[[Category: Yajima S]]
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[[Category: protein-protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:22 2008''
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Current revision

Ribonuclease from Escherichia coli complexed with its inhibtor protein

PDB ID 1tfk

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OCA

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