3R9E
Crystal structure of Microcin C7 self immunity acetyltransferase MccE in complex with coenzyme A and aspartyl sulfamoyl adenosine (DSA)
3R9E の概要
| エントリーDOI | 10.2210/pdb3r9e/pdb |
| 関連するPDBエントリー | 3R95 3R96 3R9F 3R9G |
| 分子名称 | MccE protein, COENZYME A, 5'-O-(L-alpha-aspartylsulfamoyl)adenosine, ... (4 entities in total) |
| 機能のキーワード | microcin c7, acetyltransferase, self immunity, resistance, acetyl coenzyme a, transferase |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 44554.47 |
| 構造登録者 | |
| 主引用文献 | Agarwal, V.,Metlitskaya, A.,Severinov, K.,Nair, S.K. Structural Basis for Microcin C7 Inactivation by the MccE Acetyltransferase. J.Biol.Chem., 286:21295-21303, 2011 Cited by PubMed Abstract: 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 shown previously 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 studies of the MccE acetyltransferase domain (MccE(AcTase)). 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 π-stacking interactions similar to those found in cap-binding proteins and nucleotidyltransferases. These studies provide a rationale for the observation that MccE(AcTase) can detoxify a range of aminoacylnucleotides, including those that are structurally distinct from microcin C7. PubMed: 21507941DOI: 10.1074/jbc.M111.226282 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.25 Å) |
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