6X0A

X-ray structure of a chimeric ParDE toxin-antitoxin complex from Mesorhizobium opportunistum

6X0A の概要

• エントリーDOI: 10.2210/pdb6x0a/pdb
• 分子名称: Plasmid stabilization system, Putative addiction module antidote protein, CopG/Arc/MetJ family chimera, 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE (3 entities in total)
• 機能のキーワード: toxin-antitoxin complex, toxin
• 由来する生物種: Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075); 詳細
• タンパク質・核酸の鎖数: 36
• 化学式量合計: 401623.02

構造登録者

Lite, T.L.,Grant, R.A.,Laub, M.T. (登録日: 2020-05-15, 公開日: 2020-11-25, 最終更新日: 2023-10-18)

主引用文献

Lite, T.V.,Grant, R.A.,Nocedal, I.,Littlehale, M.L.,Guo, M.S.,Laub, M.T.
Uncovering the basis of protein-protein interaction specificity with a combinatorially complete library.
Elife, 9:-, 2020

PubMed Abstract: Protein-protein interaction specificity is often encoded at the primary sequence level. However, the contributions of individual residues to specificity are usually poorly understood and often obscured by mutational robustness, sequence degeneracy, and epistasis. Using bacterial toxin-antitoxin systems as a model, we screened a combinatorially complete library of antitoxin variants at three key positions against two toxins. This library enabled us to measure the effect of individual substitutions on specificity in hundreds of genetic backgrounds. These distributions allow inferences about the general nature of interface residues in promoting specificity. We find that positive and negative contributions to specificity are neither inherently coupled nor mutually exclusive. Further, a wild-type antitoxin appears optimized for specificity as no substitutions improve discrimination between cognate and non-cognate partners. By comparing crystal structures of paralogous complexes, we provide a rationale for our observations. Collectively, this work provides a generalizable approach to understanding the logic of molecular recognition.

PubMed: 33107822
DOI: 10.7554/eLife.60924

実験手法

X-RAY DIFFRACTION (2.9 Å)