ArticlePloS one2011
Structural and sequence analysis of imelysin-like proteins implicated in bacterial iron uptake.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Time-Course Gene Expression of 'Microorganisms · 2025Article
- Differential expression of "Candidatus Liberibacter solanacearum" genes and prophage loci in different life stages of potato psyllid.Scientific reports · 2024Article
- Leptospiral imelysin (LIC_10713) is secretory, immunogenic and binds to laminin, fibronectin, and collagen IV.Applied microbiology and biotechnology · 2023Article
- Crystal structure and metal binding properties of the periplasmic iron component EfeM from Pseudomonas syringae EfeUOB/M iron-transport system.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022Article
- Extracellular Proteome Analysis Shows the Abundance of Histidine Kinase Sensor Protein, DNA Helicase, Putative Lipoprotein Containing Peptidase M75 Domain and Peptidase C39 Domain Protein inPathogens (Basel, Switzerland) · 2021Article
- Dinoroseobacter shibae Outer Membrane Vesicles Are Enriched for the Chromosome Dimer Resolution SitemSystems · 2021Article
- The Complete Genome Sequence of the Fish PathogenFrontiers in microbiology · 2017Article
- Pathogenic Leptospira interrogans exoproteins are primarily involved in heterotrophic processes.Infection and immunity · 2015Article
- Towards New Drug Targets? Function Prediction of Putative Proteins of Neisseria meningitidis MC58 and Their Virulence Characterization.Omics : a journal of integrative biology · 2015Article
- Potential impact on kidney infection: a whole-genome analysis of Leptospira santarosai serovar Shermani.Emerging microbes & infections · 2014Article
- Global gene expression changes in Candidatus Liberibacter asiaticus during the transmission in distinct hosts between plant and insect.Molecular plant pathology · 2013Article
- Staphylococcus aureus FepA and FepB proteins drive heme iron utilization in Escherichia coli.PloS one · 2013Article
- The iron-regulated staphylococcal lipoproteins.Frontiers in cellular and infection microbiology · 2012Review
Corrections and comments
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Authors and funding
15 authors at 8 institutions in 2 countries.
Funding
Abstract
Imelysin-like proteins define a superfamily of bacterial proteins that are likely involved in iron uptake. Members of this superfamily were previously thought to be peptidases and were included in the MEROPS family M75. We determined the first crystal structures of two remotely related, imelysin-like proteins. The Psychrobacter arcticus structure was determined at 2.15 Å resolution and contains the canonical imelysin fold, while higher resolution structures from the gut bacteria Bacteroides ovatus, in two crystal forms (at 1.25 Å and 1.44 Å resolution), have a circularly permuted topology. Both structures are highly similar to each other despite low sequence similarity and circular permutation. The all-helical structure can be divided into two similar four-helix bundle domains. The overall structure and the GxHxxE motif region differ from known HxxE metallopeptidases, suggesting that imelysin-like proteins are not peptidases. A putative functional site is located at the domain interface. We have now organized the known homologous proteins into a superfamily, which can be separated into four families. These families share a similar functional site, but each has family-specific structural and sequence features. These results indicate that imelysin-like proteins have evolved from a common ancestor, and likely have a conserved function.
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