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1NOV

NODAMURA VIRUS

Summary for 1NOV
Entry DOI10.2210/pdb1nov/pdb
DescriptorNODAMURA VIRUS COAT PROTEINS (2 entities in total)
Functional Keywordsinsect virus, nodamura virus, coat protein, icosahedral virus, virus
Biological sourceNodamura virus
More
Cellular locationCapsid protein beta: Virion (Potential). Peptide gamma: Virion (Potential): P12871 P12871
Total number of polymer chains6
Total formula weight129381.27
Authors
Natarajan, P.,Johnson, J.E. (deposition date: 1997-09-16, release date: 1998-01-14, Last modification date: 2024-11-06)
Primary citationZlotnick, A.,Natarajan, P.,Munshi, S.,Johnson, J.E.
Resolution of space-group ambiguity and structure determination of nodamura virus to 3.3 A resolution from pseudo-R32 (monoclinic) crystals.
Acta Crystallogr.,Sect.D, 53:738-746, 1997
Cited by
PubMed Abstract: Monoclinic crystals of nodamura virus (NOV) have two virus molecules per asymmetric unit. Packing analysis reveals a pseudo-rhombohedral (pseudo-C2 monoclinic) arrangement of particles in the actual P2(1) space group (a = 562.1, b = 354.1, c = 612.8 A, beta = 110.9 degrees ). The R32 symmetry is broken rotationally and translationally. The pseudo-symmetry of the unit cell results in three possible monoclinic origins and also restrains the four particles in the unit cell to similar orientations. NOV particles deviate by less than 3 degrees from the ideal orientations, causing overlap of peaks in the rotation function and the generation of peaks that were not interpretable as particle symmetry elements. The space-group ambiguity was resolved by analysing the relationship between the particle orientations determined by high-resolution rotation functions and the attenuation of peak heights in native Patterson maps. Particles were centered less than 1 A from the R32 special positions. Three different approaches were required to identify the correct particle center. Following the solutions of the rotation and translation problems, phases were computed using the coordinates of flock house virus (FHV), another member of this virus family. The phases were improved by real-space molecular averaging with a 120-fold non-crystallographic symmetry and by solvent flattening with a spherical mask. The final model for the NOV structure was built using the 3.3 A averaged map. While the overall subunit structure was very similar to that of other nodaviruses, FHV and black beetle virus, NOV showed distinct structural features near particle threefold and quasi-threefold axes and at the protein-RNA interfaces that are consistent with phenotype differences among the related viruses.
PubMed: 15299863
DOI: 10.1107/S0907444997007427
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.5 Å)
Structure validation

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