ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
The structure of BVU2987 from Bacteroides vulgatus reveals a superfamily of bacterial periplasmic proteins with possible inhibitory function.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Adaptive Evolution within Gut Microbiomes of Healthy People.Cell host & microbe · 2019Article
- Role of YpeB in cortex hydrolysis during germination of Bacillus anthracis spores.Journal of bacteriology · 2014Article
- Molecular characterization of novel pyridoxal-5'-phosphate-dependent enzymes from the human microbiome.Protein science : a publication of the Protein Society · 2014Article
- A sporulation-specific, sigF-dependent protein, SspA, affects septum positioning in Streptomyces coelicolor.Molecular microbiology · 2014Article
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51 authors.
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Abstract
Proteins that contain the DUF2874 domain constitute a new Pfam family PF11396. Members of this family have predominantly been identified in microbes found in the human gut and oral cavity. The crystal structure of one member of this family, BVU2987 from Bacteroides vulgatus, has been determined, revealing a β-lactamase inhibitor protein-like structure with a tandem repeat of domains. Sequence analysis and structural comparisons reveal that BVU2987 and other DUF2874 proteins are related to β-lactamase inhibitor protein, PepSY and SmpA_OmlA proteins and hence are likely to function as inhibitory proteins.
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