3r9g

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Current revision (10:53, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3r9g' size='340' side='right'caption='[[3r9g]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
<StructureSection load='3r9g' size='340' side='right'caption='[[3r9g]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3r9g]] is a 2 chain structure with sequence from [https://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=3R9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R9G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3r9g]] 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=3R9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R9G FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7MC:5-O-[(R)-[(N-ACETYL-L-ALPHA-ASPARTYL)AMINO](3-AMINOPROPOXY)PHOSPHORYL]ADENOSINE'>7MC</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
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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]] 1.35&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3r95|3r95]], [[3r96|3r96]], [[3r9e|3r9e]], [[3r9f|3r9f]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7MC:5-O-[(R)-[(N-ACETYL-L-ALPHA-ASPARTYL)AMINO](3-AMINOPROPOXY)PHOSPHORYL]ADENOSINE'>7MC</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mccE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
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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=3r9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r9g OCA], [https://pdbe.org/3r9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r9g RCSB], [https://www.ebi.ac.uk/pdbsum/3r9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r9g ProSAT]</span></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=3r9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r9g OCA], [https://pdbe.org/3r9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r9g RCSB], [https://www.ebi.ac.uk/pdbsum/3r9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r9g ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q47510_ECOLX Q47510_ECOLX]
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The antibiotic microcin C7 (McC) acts as a bacteriocide by inhibiting aspartyl tRNA synthetase, and stalling the protein translation machinery. McC is synthesized as a heptapeptide-nucleotide conjugate, which is processed by cellular peptidases within target strains to yield the biologically active compound. As unwanted processing of intact McC can result in self-toxicity, producing strains utilize multiple mechanisms for autoimmunity against processed McC. We have previously shown that the mccE gene within the biosynthetic cluster can inactivate processed McC by acetylating the antibiotic. Here, we present the characterization of this acetylation mechanism through biochemical and structural biological characterization of the acetyltransferase domain of MccE (MccEAcTase). We have also determined five crystal structures of the MccE-acetyl CoA complex with bound substrates, inhibitor and reaction product. The structural data reveal an unexpected mode of substrate recognition through pi-stacking interactions, similar to those found in cap binding proteins and nucleotidyltransferases. These studies provide a rationale for the observation that MccEAcTase can detoxify a range of aminoacyl-nucleotides, including those that are structurally distinct from microcin C7.
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Structural basis for Microcin C7 inactivation by the MccE acetyltransferase.,Agarwal V, Metlytskaya A, Severinov KV, Nair SK J Biol Chem. 2011 Apr 19. PMID:21507941<ref>PMID:21507941</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3r9g" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Agarwal, V]]
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[[Category: Agarwal V]]
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[[Category: Nair, S K]]
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[[Category: Nair SK]]
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[[Category: Acetyl coenzyme some]]
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[[Category: Acetyltransferase]]
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[[Category: Microcin c7]]
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[[Category: Resistance]]
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[[Category: Self immunity]]
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[[Category: Transferase-transferase inhibitor complex]]
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Current revision

Crystal structure of Microcin C7 self immunity acetyltransferase MccE in complex with Coenzyme A and processed Microcin C7 antibiotic

PDB ID 3r9g

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OCA

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