3RER
Crystal structure of E. coli Hfq in complex with AU6A RNA and ADP
3RER の概要
| エントリーDOI | 10.2210/pdb3rer/pdb |
| 関連するPDBエントリー | 3RES |
| 分子名称 | Protein hfq, 5'-R(*AP*UP*UP*UP*UP*UP*UP*A)-3', ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total) |
| 機能のキーワード | adp, hfq, dsra, sm fold, rna chaperone, atp and rna binding, chaperone-rna complex, chaperone/rna |
| 由来する生物種 | Escherichia coli 詳細 |
| タンパク質・核酸の鎖数 | 7 |
| 化学式量合計 | 48588.39 |
| 構造登録者 | |
| 主引用文献 | Wang, W.,Wang, L.,Zou, Y.,Zhang, J.,Gong, Q.,Wu, J.,Shi, Y. Cooperation of Escherichia coli Hfq hexamers in DsrA binding. Genes Dev., 25:2106-2117, 2011 Cited by PubMed Abstract: Hfq is a bacterial post-transcriptional regulator. It facilitates base-pairing between sRNA and target mRNA. Hfq mediates DsrA-dependent translational activation of rpoS mRNA at low temperatures. rpoS encodes the stationary-phase σ factor σ(S), which is the central regulator in general stress response. However, structural information on Hfq-DsrA interaction is not yet available. Although Hfq is reported to hydrolyze ATP, the ATP-binding site is still unknown. Here, we report a ternary crystal complex structure of Escherichia coli Hfq bound to a major Hfq recognition region on DsrA (AU(6)A) together with ADP, and a crystal complex structure of Hfq bound to ADP. AU(6)A binds to the proximal and distal sides of two Hfq hexamers. ADP binds to a purine-selective site on the distal side and contacts conserved arginine or glutamine residues on the proximal side of another hexamer. This binding mode is different from previously postulated. The cooperation of two different Hfq hexamers upon nucleic acid binding in solution is verified by fluorescence polarization and solution nuclear magnetic resonance (NMR) experiments using fragments of Hfq and DsrA. Fluorescence resonance energy transfer conducted with full-length Hfq and DsrA also supports cooperation of Hfq hexamers upon DsrA binding. The implications of Hfq hexamer cooperation have been discussed. PubMed: 21979921DOI: 10.1101/gad.16746011 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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