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3t5m

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Crystal structure of the S112A mutant of mycrocine immunity protein (MccF) with AMP

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 <StructureSection load='3t5m' size='340' side='right'caption='[[3t5m]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3t5m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_(strain_ames) Bacillus anthracis (strain ames)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T5M FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3t5m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_str._Ames Bacillus anthracis str. Ames]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T5M FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.749&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAS1809, BA_1949, GBAA_1949 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=198094 Bacillus anthracis (strain Ames)])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=3t5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t5m OCA], [https://pdbe.org/3t5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t5m RCSB], [https://www.ebi.ac.uk/pdbsum/3t5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t5m ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/A0A6L8PEJ7_BACAN A0A6L8PEJ7_BACAN]
-Microcin C (McC) is heptapeptide adenylate antibiotic produced by Escherichia coli strains carrying the mccABCDEF gene cluster encoding enzymes, in addition to the heptapeptide structural gene mccA, necessary for McC biosynthesis and self-immunity of the producing cell. The heptapeptide facilitates McC transport into susceptible cells, where it is processed releasing a non-hydrolyzable aminoacyl adenylate that inhibits an essential aminoacyl-tRNA synthetase. The self-immunity gene mccF encodes a specialized serine peptidase that cleaves an amide bond connecting the peptidyl or aminoacyl moieties of, respectively, intact and processed McC with the nucleotidyl moiety. Most mccF orthologs from organisms other than E. coli are not linked to the McC biosynthesis gene cluster. Here, we show that a protein product of one such gene, MccF from Bacillus anthracis (BaMccF), is able to cleave intact and processed McC, and we present a series of structures of this protein. Structural analysis of apo-BaMccF and its adenosine monophosphate complex reveals specific features of MccF-like peptidases that allow them to interact with substrates containing nucleotidyl moieties. Sequence analyses and phylogenetic reconstructions suggest that several distinct subfamilies form the MccF clade of the large S66 family of bacterial serine peptidases. We show that various representatives of the MccF clade can specifically detoxify non-hydrolyzable aminoacyl adenylates differing in their aminoacyl moieties. We hypothesize that bacterial mccF genes serve as a source of bacterial antibiotic resistance.
-Structural and Functional Characterization of Microcin C Resistance Peptidase MccF from Bacillus anthracis.,Nocek B, Tikhonov A, Babnigg G, Gu M, Zhou M, Makarova KS, Vondenhoff G, Aerschot AV, Kwon K, Anderson WF, Severinov K, Joachimiak A J Mol Biol. 2012 Apr 16. PMID:22516613<ref>PMID:22516613</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3t5m" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
+[[Category: Bacillus anthracis str. Ames]]
 [[Category: Large Structures]]
-[[Category: Anderson, W F]]
+[[Category: Anderson WF]]
-[[Category: Structural genomic]]
+[[Category: Gu M]]
-[[Category: Gu, M]]
+[[Category: Joachimiak A]]
-[[Category: Joachimiak, A]]
+[[Category: Nocek B]]
-[[Category: Nocek, B]]
+[[Category: Zhou M]]
-[[Category: Zhou, M]]
-[[Category: Amp]]
-[[Category: Csgid]]
-[[Category: Immune system]]
-[[Category: Mccf]]

3t5m

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Crystal structure of the S112A mutant of mycrocine immunity protein (MccF) with AMP

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