ArticleActa crystallographica. Section F, Structural biology communications2014
Structure of Rhodococcus equi virulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs.
Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 19 citations in OpenAlex.
- Single mutations to tyrosine or glutamate improve the crystallizability and crystal diffraction properties of a flexible two-domain protein.Acta crystallographica. Section F, Structural biology communications · 2026Article
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- The crystal structure of DynF from the dynemicin-biosynthesis pathway of Micromonospora chersina.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB.Acta crystallographica. Section F, Structural biology communications · 2021Article
- The pathogenic actinobacterium Rhodococcus equi: what's in a name?Molecular microbiology · 2019Review
- VapA of Rhodococcus equi binds phosphatidic acid.Molecular microbiology · 2018Article
- Identification of a VapA virulence factor functional homolog in Rhodococcus equi isolates housing the pVAPB plasmid.PloS one · 2018Article
- The Rhodococcus equi virulence protein VapA disrupts endolysosome function and stimulates lysosome biogenesis.MicrobiologyOpen · 2017Article
- Structural characterisation of the virulence-associated protein VapG from the horse pathogen Rhodococcus equi.Veterinary microbiology · 2015Article
- Transcriptome reprogramming by plasmid-encoded transcriptional regulators is required for host niche adaption of a macrophage pathogen.Infection and immunity · 2015Article
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4 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Members of the virulence-associated protein (Vap) family from the pathogen Rhodococcus equi regulate virulence in an unknown manner. They do not share recognizable sequence homology with any protein of known structure. VapB and VapA are normally associated with isolates from pigs and horses, respectively. To contribute to a molecular understanding of Vap function, the crystal structure of a protease-resistant VapB fragment was determined at 1.4 Å resolution. The structure was solved by SAD phasing employing the anomalous signal of one endogenous S atom and two bound Co ions with low occupancy. VapB is an eight-stranded antiparallel β-barrel with a single helix. Structural similarity to avidins suggests a potential binding function. Unlike other eight- or ten-stranded β-barrels found in avidins, bacterial outer membrane proteins, fatty-acid-binding proteins and lysozyme inhibitors, Vaps do not have a next-neighbour arrangement but consist of two Greek-key motifs with strand order 41238567, suggesting an unusual or even unique topology.
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