3MUR

Crystal Structure of the C92U mutant c-di-GMP riboswith bound to c-di-GMP

3MUR の概要

• エントリーDOI: 10.2210/pdb3mur/pdb
• 関連するPDBエントリー: 3IRW 3MUM 3MUT 3MUV 3MXH
• 分子名称: U1 small nuclear ribonucleoprotein A, C92U mutant c-di-GMP riboswitch, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one), ... (5 entities in total)
• 機能のキーワード: rna, riboswitch, c-di-gmp, rna binding protein-rna complex, rna binding protein/rna
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P09012
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42023.09

構造登録者

Strobel, S.A.,Smith, K.D. (登録日: 2010-05-03, 公開日: 2010-08-25, 最終更新日: 2023-09-06)

主引用文献

Smith, K.D.,Lipchock, S.V.,Livingston, A.L.,Shanahan, C.A.,Strobel, S.A.
Structural and biochemical determinants of ligand binding by the c-di-GMP riboswitch .
Biochemistry, 49:7351-7359, 2010

PubMed Abstract: The bacterial second messenger c-di-GMP is used in many species to control essential processes that allow the organism to adapt to its environment. The c-di-GMP riboswitch (GEMM) is an important downstream target in this signaling pathway and alters gene expression in response to changing concentrations of c-di-GMP. The riboswitch selectively recognizes its second messenger ligand primarily through contacts with two critical nucleotides. However, these two nucleotides are not the most highly conserved residues within the riboswitch sequence. Instead, nucleotides that stack with c-di-GMP and that form tertiary RNA contacts are the most invariant. Biochemical and structural evidence reveals that the most common natural variants are able to make alternative pairing interactions with both guanine bases of the ligand. Additionally, a high-resolution (2.3 A) crystal structure of the native complex reveals that a single metal coordinates the c-di-GMP backbone. Evidence is also provided that after transcription of the first nucleotide on the 3'-side of the P1 helix, which is predicted to be the molecular switch, the aptamer is functional for ligand binding. Although large energetic effects occur when several residues in the RNA are altered, mutations at the most conserved positions, rather than at positions that base pair with c-di-GMP, have the most detrimental effects on binding. Many mutants retain sufficient c-di-GMP affinity for the RNA to remain biologically relevant, which suggests that this motif is quite resilient to mutation.

PubMed: 20690679
DOI: 10.1021/bi100671e

実験手法

X-RAY DIFFRACTION (3 Å)