2a6r: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2a6r]] is a 6 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=2A6R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A6R FirstGlance]. <br> | <table><tr><td colspan='2'>[[2a6r]] is a 6 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=2A6R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A6R FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2a6q|2a6q]], [[2a6s|2a6s]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2a6q|2a6q]], [[2a6s|2a6s]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yoeB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yoeB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a6r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2a6r RCSB], [http://www.ebi.ac.uk/pdbsum/2a6r PDBsum]</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=2a6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a6r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2a6r RCSB], [http://www.ebi.ac.uk/pdbsum/2a6r PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/YOEB_ECOLI YOEB_ECOLI]] Toxic component of a toxin-antitoxin (TA) module. Its mode of function is controversial; it has been proposed to be an mRNA interferase but also an inhibitor of translation initiation. When overproduced in wild-type cells, inhibits bacterial growth and translation by cleavage of mRNA molecules while it has a weak effect on colony forming ability. Overproduction of Lon protease specifically activates YoeB-dependent mRNA cleavage, leading to lethality. YefM binds to the promoter region of the yefM-yeoB operon to repress transcription, YeoB acts as a corepressor.<ref>PMID:14672926</ref> <ref>PMID:15009896</ref> <ref>PMID:17170003</ref> <ref>PMID:18854355</ref> <ref>PMID:19028895</ref> <ref>PMID:19124462</ref> <ref>PMID:19400780</ref> <ref>PMID:16109374</ref> Shown in vitro to be an mRNA interferase that requires translation for substrate cleavage; if the mRNA is mutated so as to not be translatable it is no longer cleaved. Cleavage only occurs within translated regions. Has RNase activity and preferentially cleaves at the 3'-end of purine ribonucleotides.<ref>PMID:14672926</ref> <ref>PMID:15009896</ref> <ref>PMID:17170003</ref> <ref>PMID:18854355</ref> <ref>PMID:19028895</ref> <ref>PMID:19124462</ref> <ref>PMID:19400780</ref> <ref>PMID:16109374</ref> Also shown in vitro to be a translation initiation blocker. Binds to the 70S ribosome and 50S ribosomal subunit; binding is inhibited by hygromycin A and tetracycline, both of which bind to the 30S subunit in the A site. Thus YoeB is located at the interface between 50S and 30S ribosomes and interacts with the A site where it cleaves mRNA, blocking translation initiation.<ref>PMID:14672926</ref> <ref>PMID:15009896</ref> <ref>PMID:17170003</ref> <ref>PMID:18854355</ref> <ref>PMID:19028895</ref> <ref>PMID:19124462</ref> <ref>PMID:19400780</ref> <ref>PMID:16109374</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 31: | Line 33: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Hanaoka, F | [[Category: Hanaoka, F]] | ||
[[Category: Kamada, K | [[Category: Kamada, K]] | ||
[[Category: Addiction module]] | [[Category: Addiction module]] | ||
[[Category: Antitoxin]] | [[Category: Antitoxin]] | ||
Revision as of 20:49, 24 December 2014
Crystal structure of YoeB under PEG condition
| ||||||||||||
