Crystal Structure of an Unusual Single-Stranded DNA-Binding Protein Encoded by Staphylococcal Cassette Chromosome Elements
| Autor: | Phoebe A. Rice, Ying Z. Pigli, Ignacio Mir-Sanchis |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
DNA Replication DNA Bacterial Methicillin-Resistant Staphylococcus aureus Models Molecular Protein Conformation alpha-Helical 030106 microbiology Genetic Vectors DNA Single-Stranded Gene Expression Crystallography X-Ray DNA-binding protein Article Substrate Specificity 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Structural Biology Escherichia coli Protein Interaction Domains and Motifs Amino Acid Sequence Cloning Molecular Molecular Biology Gene Conserved Sequence Genetics Binding Sites Chemistry SCCmec DNA replication Cooperative binding Recombinant Proteins DNA-Binding Proteins 030104 developmental biology Horizontal gene transfer Methicillin Resistance Protein Conformation beta-Strand Mobile genetic elements Hydrophobic and Hydrophilic Interactions Sequence Alignment DNA Protein Binding |
| Zdroj: | Structure (London, England : 1993). 26(8) |
| ISSN: | 1878-4186 |
| Popis: | Summary Methicillin-resistant Staphylococcus aureus is a global public health threat. Methicillin resistance is carried on mobile genetic elements belonging to the staphylococcal cassette chromosome (SCC) family. The molecular mechanisms that SCC elements exploit for stable maintenance and for horizontal transfer are poorly understood. Previously, we identified several conserved SCC genes with putative functions in DNA replication, including lp1413, which we found encodes a single-stranded DNA (ssDNA)-binding protein. We report here the 2.18 A crystal structure of LP1413, which shows that it adopts a winged helix-turn-helix fold rather than the OB-fold normally seen in replication-related ssDNA-binding proteins. However, conserved residues form a hydrophobic pocket not normally found in winged helix-turn-helix domains. LP1413 also has a conserved but disordered C-terminal tail. As deletion of the tail does not significantly affect cooperative binding to ssDNA, we propose that it mediates interactions with other proteins. LP1413 could play several different roles in vivo. |
| Databáze: | OpenAIRE |
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