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==Ribonuclease from Escherichia coli complexed with its inhibtor protein==
==Ribonuclease from Escherichia coli complexed with its inhibtor protein==
<StructureSection load='1tfk' size='340' side='right' caption='[[1tfk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1tfk' size='340' side='right'caption='[[1tfk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1tfk]] is a 2 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TFK FirstGlance]. <br>
<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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tfo|1tfo]]</td></tr>
<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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">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])</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=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>
<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=1tfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tfk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tfk RCSB], [http://www.ebi.ac.uk/pdbsum/1tfk PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tf/1tfk_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tf/1tfk_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata 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=1tfk ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:15336558<ref>PMID:15336558</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Colicin|Colicin]]
*[[Colicin 3D structures|Colicin 3D structures]]
*[[Colicin Immunity Protein|Colicin Immunity Protein]]
*[[Colicin immunity protein 3D structures|Colicin immunity protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Hidaka, M]]
[[Category: Large Structures]]
[[Category: Kezuka, Y]]
[[Category: Hidaka M]]
[[Category: Masaki, H]]
[[Category: Kezuka Y]]
[[Category: Nakanishi, K]]
[[Category: Masaki H]]
[[Category: Nonaka, T]]
[[Category: Nakanishi K]]
[[Category: Ogawa, T]]
[[Category: Nonaka T]]
[[Category: Ohsawa, K]]
[[Category: Ogawa T]]
[[Category: Takahashi, K]]
[[Category: Ohsawa K]]
[[Category: Yajima, S]]
[[Category: Takahashi K]]
[[Category: Protein-protein complex]]
[[Category: Yajima S]]
[[Category: Toxin-toxin inhibitor complex]]

Latest revision as of 11:39, 14 February 2024

Ribonuclease from Escherichia coli complexed with its inhibtor proteinRibonuclease from Escherichia coli complexed with its inhibtor protein

Structural highlights

1tfk is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CEAD_ECOLX Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria. Colicin D inhibits protein synthesis.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1tfk, resolution 2.10Å

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OCA
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