6ajn
From Proteopedia
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<StructureSection load='6ajn' size='340' side='right' caption='[[6ajn]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='6ajn' size='340' side='right' caption='[[6ajn]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6ajn]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AJN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AJN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ajn]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AJN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AJN FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BWP17_00640, CVH05_12355 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), ybl13, ybl13_1, A8G17_04185, AA102_09360, AC789_1c38270, ACN002_3543, ACN81_27750, ACU90_15595, AM270_07745, ARC77_13665, AU473_04475, B1K96_23180, B1K96_30445, BHS81_20640, BIZ41_06975, BK292_07330, BMT53_16880, BN17_33961, BTQ04_07040, BWP17_00645, C5P43_28430, C5Y95_12220, C6986_22200, C7B02_13210, COD46_18440, CR538_01655, CVH05_12360, CXB56_05005, ERS085366_00076, ERS085374_01548, ERS085383_01733, ERS085404_01502, RX35_03224, SAMEA3472031_01067, SAMEA3472035_01725, SAMEA3472046_03089, SAMEA3472089_01664, SAMEA3472114_02231, SAMEA3472140_01493, SAMEA3472152_01575, SAMEA3484446_02490, SAMEA3485110_02685, SAMEA3753064_01902, SAMEA3753068_03922, SAMEA3753290_02356 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=6ajn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ajn OCA], [http://pdbe.org/6ajn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ajn RCSB], [http://www.ebi.ac.uk/pdbsum/6ajn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ajn 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=6ajn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ajn OCA], [http://pdbe.org/6ajn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ajn RCSB], [http://www.ebi.ac.uk/pdbsum/6ajn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ajn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | AtaT-AtaR is an enterohemorrhagic Escherichia coli toxin-antitoxin system that modulates cellular growth under stress conditions. AtaT and AtaR act as a toxin and its repressor, respectively. AtaT is a member of the GNAT family, and the dimeric AtaT acetylates the alpha-amino group of the aminoacyl moiety of methionyl initiator tRNA(fMet), thereby inhibiting translation initiation. The crystallographic analysis of the AtaT-AtaR complex revealed that the AtaT-AtaR proteins form a heterohexameric [AtaT-(AtaR4)-AtaT] complex, where two V-shaped AtaR dimers bridge two AtaT molecules. The N-terminal region of AtaR is required for its dimerization, and the C-terminal region of AtaR interacts with AtaT. The two AtaT molecules are spatially separated in the AtaT-AtaR complex. AtaT alone forms a dimer in solution, which is enzymatically active. The present structure, in which AtaR prevents AtaT from forming an active dimer, reveals the molecular basis of the AtaT toxicity repression by the antitoxin AtaR. | ||
| + | |||
| + | Crystal Structure of the Enterohemorrhagic Escherichia coli AtaT-AtaR Toxin-Antitoxin Complex.,Yashiro Y, Yamashita S, Tomita K Structure. 2018 Nov 21. pii: S0969-2126(18)30424-6. doi:, 10.1016/j.str.2018.11.005. PMID:30612860<ref>PMID:30612860</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6ajn" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Tomita, K]] | [[Category: Tomita, K]] | ||
[[Category: Yamashita, S]] | [[Category: Yamashita, S]] | ||
Revision as of 09:43, 13 February 2019
Crystal structure of AtaTR bound with AcCoA
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