2Q82

Crystal structure of core protein P7 from Pseudomonas phage phi12. Northeast Structural Genomics Target OC1

2Q82 の概要

• エントリーDOI: 10.2210/pdb2q82/pdb
• 分子名称: Core protein P7 (2 entities in total)
• 機能のキーワード: p7, core protein, nesg, oc1, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, structural protein
• 由来する生物種: Pseudomonas phage phi12
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14450.37

構造登録者

Benach, J.,Eryilmaz, E.,Su, M.,Seetharaman, J.,Wei, H.,Gottlieb, P.,Hunt, J.F.,Ghose, R.,Northeast Structural Genomics Consortium (NESG) (登録日: 2007-06-08, 公開日: 2007-08-07, 最終更新日: 2024-10-30)

主引用文献

Eryilmaz, E.,Benach, J.,Su, M.,Seetharaman, J.,Dutta, K.,Wei, H.,Gottlieb, P.,Hunt, J.F.,Ghose, R.
Structure and dynamics of the P7 protein from the bacteriophage phi 12.
J.Mol.Biol., 382:402-422, 2008

PubMed Abstract: Cystoviruses are a class of enveloped double-stranded RNA viruses that use a multiprotein polymerase complex (PX) to replicate and transcribe the viral genome. Although the structures of the polymerase and ATPase components of the cystoviral PX are known and their functional behavior is understood to a large extent, no atomic-resolution structural information is available for the major capsid protein P1 that defines the overall structure and symmetry of the viral capsid and the essential protein P7. Toward obtaining a complete structural and functional understanding of the cystoviral PX, we have obtained the structure of P7 from the cystovirus phi 12 at a resolution of 1.8 A. The N-terminal core region (1-129) of P7 forms a novel homodimeric alpha/beta-fold having structural similarities with BRCT domains implicated in multiple protein-protein interactions in DNA repair proteins. Our results, combined with the known role of P7 in stabilizing the nucleation complex during capsid assembly, hint toward its participation in key protein-protein interactions within the cystoviral PX. Additionally, we have found through solution NMR studies that the C-terminal tail of P7 (130-169) that is essential for virus viability, although highly disordered, contains a nascent helix. We demonstrate for the first time, through NMR titrations, that P7 is capable of interacting with RNA. We find that both the N-terminal core and the dynamic C-terminal tail of P7 play a role in RNA recognition. This interaction leads to a significant reduction of the degree of disorder in the C-terminal tail. Given the requirement of P7 in maintaining genome packaging efficiency and transcriptional fidelity, our data suggest a central biological role for P7-RNA interactions.

PubMed: 18647606
DOI: 10.1016/j.jmb.2008.07.006

実験手法

X-RAY DIFFRACTION (1.83 Å)