5FGU

Structure of Sda1 nuclease apoprotein as an EGFP fixed-arm fusion

5FGU の概要

• エントリーDOI: 10.2210/pdb5fgu/pdb
• 関連するPDBエントリー: 5FGW
• 分子名称: Green fluorescent protein,Extracellular streptodornase D, SULFATE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: beta-beta-alpha metal finger nuclease, sequence nonspecific dna binding, metal binding protein, dna binding protein, metal binding
• 由来する生物種: Aequorea victoria (Jellyfish); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 64688.45

構造登録者

Moon, A.F.,Krahn, J.M.,Xun, L.,Cuneo, M.J.,Pedersen, L.C. (登録日: 2015-12-21, 公開日: 2016-03-30, 最終更新日: 2024-10-23)

主引用文献

Moon, A.F.,Krahn, J.M.,Lu, X.,Cuneo, M.J.,Pedersen, L.C.
Structural characterization of the virulence factor Sda1 nuclease from Streptococcus pyogenes.
Nucleic Acids Res., 44:3946-3957, 2016

PubMed Abstract: Infection by Group A Streptococcus pyogenes (GAS) is a leading cause of severe invasive disease in humans, including streptococcal toxic shock syndrome and necrotizing fasciitis. GAS infections lead to nearly 163,000 annual deaths worldwide. Hypervirulent strains of S. pyogenes have evolved a plethora of virulence factors that aid in disease-by promoting bacterial adhesion to host cells, subsequent invasion of deeper tissues and blocking the immune system's attempts to eradicate the infection. Expression and secretion of the extracellular nuclease Sda1 is advantageous for promoting bacterial dissemination throughout the host organism, and evasion of the host's innate immune response. Here we present two crystal structures of Sda1, as well as biochemical studies to address key structural features and surface residues involved in DNA binding and catalysis. In the active site, Asn211 is observed to directly chelate a hydrated divalent metal ion and Arg124, on the putative substrate binding loop, likely stabilizes the transition state during phosphodiester bond cleavage. These structures provide a foundation for rational drug design of small molecule inhibitors to be used in prevention of invasive streptococcal disease.

PubMed: 26969731
DOI: 10.1093/nar/gkw143

実験手法

X-RAY DIFFRACTION (1.896 Å)