Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages

Autor: Andris Kazaks, Loren B. Andreas, Christoph A. Diebolder, Inara Akopjana, Kristaps Jaudzems, Janis Rumnieks, Jan Stanek, Svetlana Kotelovica, Mihails Shishovs, Kaspars Tars, Guido Pintacuda, Roman I. Koning
Přispěvatelé: Latvian Biomed Res & Study Ctr, Netherlands Ctr Electron Nanoscopy, Leiden University, Solid-State NMR Methods for Materials - Méthodes de RMN à l'état solide pour les matériaux, Institut des Sciences Analytiques (ISA), Institut de Chimie du CNRS (INC)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Biological Solid-State NMR Methods - Méthodes de RMN à l'état solide en biologie, Dept Cell Biol, Dept Mol Biol, University of Latvia (LU), The study was supported by grant 12.094 from the Latvian Council of Sciences, grant 2010/0314/2DP/2.1.1.1.0/10/APIA/VIAA/052 from the European Regional Development Fund, grant 7869 from Biostruct-X, and the Latvian French cooperation program Osmosis. This research has been executed with the support of NeCEN, the Netherlands Centre for Electron Nanoscopy, Leiden, NL, and of NWO, the Netherlands Organisation for Scientific Research, and is partly financed by the European Regional Development Fund of the European Commission.
Rok vydání: 2016
Předmět:
0301 basic medicine
Models
Molecular
RNA bacteriophage
Viral protein
Cryo-electron microscopy
Protein Conformation
010402 general chemistry
medicine.disease_cause
Crystallography
X-Ray
01 natural sciences
virus-like particle
Bacteriophage
03 medical and health sciences
Structural Biology
[CHIM.ANAL]Chemical Sciences/Analytical chemistry
Leviviridae
medicine
RNA Viruses
Bacteriophages
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biochemistry [q-bio.BM]
Molecular Biology
Protein secondary structure
biology
Cryoelectron Microscopy
RNA
[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Molecular biology
circular permutation
RNA Phages
Circular permutation in proteins
biology.organism_classification
3. Good health
0104 chemical sciences
Crystallography
030104 developmental biology
coat protein
Biophysics
Capsid Proteins
Zdroj: Journal of Molecular Biology, 428(21), 4267-4279
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2016, 428 (21), pp.4267-4279. ⟨10.1016/j.jmb.2016.08.025⟩
ISSN: 1089-8638
0022-2836
DOI: 10.1016/j.jmb.2016.08.025⟩
Popis: We are thankful to the MAX-lab staff for their support during our visit at the synchrotron.; International audience; AP205 is a single-stranded RNA bacteriophage that has a coat protein sequence not similar to any other known single-stranded RNA phage. Here, we report an atomic-resolution model of the AP205 virus-like particle based on a crystal structure of an unassembled coat protein dimer and a cryo-electron microscopy reconstruction of the assembled particle, together with secondary structure information from site-specific solid-state NMR data. The AP205 coat protein dimer adopts the conserved Leviviridae coat protein fold except for the N-terminal region, which forms a beta-hairpin in the other known single-stranded RNA phages. AP205 has a similar structure at the same location formed by N- and C-terminal beta-strands, making it a circular permutant compared to the other coat proteins. The permutation moves the coat protein termini to the most surface-exposed part of the assembled particle, which explains its increased tolerance to long N- and C-terminal fusions.
Databáze: OpenAIRE
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