4R2H
The Crystal Structure of B204, the DNA-packaging ATPase from Sulfolobus Turreted Icosahedral Virus
Summary for 4R2H
| Entry DOI | 10.2210/pdb4r2h/pdb |
| Related | 4R2I |
| Descriptor | STIV B204 ATPase, ZINC ION (3 entities in total) |
| Functional Keywords | walker a motif, walker b motif, arginine finger, p-loop atpase, aaa atpase, dna-dependent atpase, viral protein |
| Biological source | Sulfolobus turreted icosahedral virus 1 |
| Total number of polymer chains | 1 |
| Total formula weight | 24889.22 |
| Authors | Dellas, N.,Nicolay, S.J.,Young, M.J. (deposition date: 2014-08-12, release date: 2016-01-13, Last modification date: 2024-02-28) |
| Primary citation | Dellas, N.,Snyder, J.C.,Dills, M.,Nicolay, S.J.,Kerchner, K.M.,Brumfield, S.K.,Lawrence, C.M.,Young, M.J. Structure-Based Mutagenesis of Sulfolobus Turreted Icosahedral Virus B204 Reveals Essential Residues in the Virion-Associated DNA-Packaging ATPase. J.Virol., 90:2729-2739, 2015 Cited by PubMed Abstract: Sulfolobus turreted icosahedral virus (STIV), an archaeal virus that infects the hyperthermoacidophile Sulfolobus solfataricus, is one of the most well-studied viruses of the domain Archaea. STIV shares structural, morphological, and sequence similarities with viruses from other domains of life, all of which are thought to belong to the same viral lineage. Several of these common features include a conserved coat protein fold, an internal lipid membrane, and a DNA-packaging ATPase. B204 is the ATPase encoded by STIV and is thought to drive packaging of viral DNA during the replication process. Here, we report the crystal structure of B204 along with the biochemical analysis of B204 mutants chosen based on structural information and sequence conservation patterns observed among members of the same viral lineage and the larger FtsK/HerA superfamily to which B204 belongs. Both in vitro ATPase activity assays and transfection assays with mutant forms of B204 confirmed the essentiality of conserved and nonconserved positions. We also have identified two distinct particle morphologies during an STIV infection that differ in the presence or absence of the B204 protein. The biochemical and structural data presented here are not only informative for the STIV replication process but also can be useful in deciphering DNA-packaging mechanisms for other viruses belonging to this lineage. PubMed: 26699645DOI: 10.1128/JVI.02435-15 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
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