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7N0J

Structure of YebY from E. coli K12

7N0J の概要
エントリーDOI10.2210/pdb7n0j/pdb
分子名称YebY (2 entities in total)
機能のキーワードperiplasmic protein, unknown function
由来する生物種Escherichia coli K-12
タンパク質・核酸の鎖数12
化学式量合計137552.09
構造登録者
Hadley, R.C.,Rosenzweig, A.C. (登録日: 2021-05-25, 公開日: 2022-03-09, 最終更新日: 2024-10-23)
主引用文献Hadley, R.C.,Zhitnitsky, D.,Livnat-Levanon, N.,Masrati, G.,Vigonsky, E.,Rose, J.,Ben-Tal, N.,Rosenzweig, A.C.,Lewinson, O.
The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery.
J.Biol.Chem., 298:101445-101445, 2022
Cited by
PubMed Abstract: The Escherichia coli yobA-yebZ-yebY (AZY) operon encodes the proteins YobA, YebZ, and YebY. YobA and YebZ are homologs of the CopC periplasmic copper-binding protein and the CopD putative copper importer, respectively, whereas YebY belongs to the uncharacterized Domain of Unknown Function 2511 family. Despite numerous studies of E. coli copper homeostasis and the existence of the AZY operon in a range of bacteria, the operon's proteins and their functional roles have not been explored. In this study, we present the first biochemical and functional studies of the AZY proteins. Biochemical characterization and structural modeling indicate that YobA binds a single Cu ion with high affinity. Bioinformatics analysis shows that YebY is widespread and encoded either in AZY operons or in other genetic contexts unrelated to copper homeostasis. We also determined the 1.8 Å resolution crystal structure of E. coli YebY, which closely resembles that of the lantibiotic self-resistance protein MlbQ. Two strictly conserved cysteine residues form a disulfide bond, consistent with the observed periplasmic localization of YebY. Upon treatment with reductants, YebY binds Cu and Cu with low affinity, as demonstrated by metal-binding analysis and tryptophan fluorescence. Finally, genetic manipulations show that the AZY operon is not involved in copper tolerance or antioxidant defense. Instead, YebY and YobA are required for the activity of the copper-related NADH dehydrogenase II. These results are consistent with a potential role of the AZY operon in copper delivery to membrane proteins.
PubMed: 34822841
DOI: 10.1016/j.jbc.2021.101445
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.88 Å)
構造検証レポート
Validation report summary of 7n0j
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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