Structure of D-63 from Sulfolobus Spindle-Shaped Virus 1: Surface Properties of the Dimeric Four-Helix Bundle Suggest an Adaptor Protein Function
| Autor: | Mark J. Young, Daniel Kümmel, Paul Kraft, George H. Gauss, C. Martin Lawrence, Blake Wiedenheft, Andrea Oeckinghaus |
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| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Protein Conformation Surface Properties Viral protein Stereochemistry Immunology Fuselloviridae Crystallography X-Ray medicine.disease_cause Antiparallel (biochemistry) Microbiology Structure-Activity Relationship Viral Proteins Virology medicine Amino Acid Sequence Helix-Turn-Helix Motifs Helix bundle biology Structure and Assembly Signal transducing adaptor protein biology.organism_classification Sulfolobus Macromolecular assembly Biochemistry Insect Science Proteome Carrier Proteins Crystallization Dimerization Sequence Alignment |
| Zdroj: | Journal of Virology. 78:7438-7442 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.78.14.7438-7442.2004 |
| Popis: | Sulfolobus spindle-shaped virus 1 (SSV1) and its fusellovirus homologues can be found in many acidic (pH ≤ 4.0) hot springs (≥70°C) around the world. SSV1 contains a 15.5-kb double-stranded DNA genome that encodes 34 proteins with greater than 50 amino acids. A site-specific integrase and a DnaA-like protein have been previously identified by sequence homology, and three structural proteins have been isolated from purified virus and identified by N-terminal sequencing (VP1, VP2, and VP3). The functions of the remaining 29 proteins are currently unknown. To assign functions to these proteins, we have initiated biochemical and structural studies on the SSV1 proteome. Here we report the structure of SSV1 D-63. The structure reveals a helix-turn-helix motif that dimerizes to form an antiparallel four-helix bundle. Mapping residues conserved among three fusellovirus isolates onto the structure shows that one face of the rod-shaped molecule is highly conserved. This conserved surface spans the dimer axis and thus exhibits 2-fold symmetry. Two smaller conserved patches, also related by 2-fold symmetry, are found on the opposite face of the molecule. All of these conserved surfaces are devoid of clefts or pockets typically used to bind small molecules, suggesting that D-63 may function as an adaptor protein in macromolecular assembly. |
| Databáze: | OpenAIRE |
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