ArticleStructure (London, England : 1993)2018
Crystal Structure of an Unusual Single-Stranded DNA-Binding Protein Encoded by Staphylococcal Cassette Chromosome Elements.
Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Progress in the Prevalence, Classification and Drug Resistance Mechanisms of Methicillin-ResistantInfection and drug resistance · 2023Review
- Staphylococcal self-loading helicases couple the staircase mechanism with inter domain high flexibility.Nucleic acids research · 2022Article
- A Novel Family of Winged-Helix Single-Stranded DNA-Binding Proteins from Archaea.International journal of molecular sciences · 2022Article
- A novel DNA primase-helicase pair encoded by SCCeLife · 2020Article
- Target highlights in CASP13: Experimental target structures through the eyes of their authors.Proteins · 2019Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
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 Å 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.
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