ArticlePloS one2011
Structural analysis of papain-like NlpC/P60 superfamily enzymes with a circularly permuted topology reveals potential lipid binding sites.
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 24 papers.
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Who cites it
24 citing papers in PubMed.
- Systematic discovery of circular permutations across the protein universe using CIRPIN.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Reconstitution of the LnsAB lipoprotein N-acylation system complex from Staphylococcus aureus and characterization of substrate preference.The Journal of biological chemistry · 2026Article
- Systematic identification of Salmonella T6SS effectors uncovers diverse new families and lipid-targeting activities.PLoS biology · 2026Article
- Transcriptome-guided discovery of novel plant-associated genes in a rhizosphere Pseudomonas.Microbiome · 2025Article
- CIRPIN: Learning Circular Permutation-Invariant Representations to Uncover Putative Protein Homologs.bioRxiv : the preprint server for biology · 2025Article
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- Functional annotation of uncharacterized proteins from Fusobacterium nucleatum: identification of virulence factors.Genomics & informatics · 2023Article
- Peptidoglycan NlpC/P60 peptidases in bacterial physiology and host interactions.Cell chemical biology · 2023Review
- Article
- Cln5 represents a new type of cysteine-basedScience advances · 2022Article
- Article
- LipoproteinmBio · 2020Article
- Envelope stress responses defend against type six secretion system attacks independently of immunity proteins.Nature microbiology · 2020Article
- A second RNA-binding protein is essential for ethanol tolerance provided by the bacterial OLE ribonucleoprotein complex.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Transcriptomic analysis of human norovirus NS1-2 protein highlights a multifunctional role in murine monocytes.BMC genomics · 2017Article
- Antibacterial activity of a cell wall hydrolase from Lactobacillus paracasei NRRL B-50314 produced by recombinant Bacillus megaterium.Journal of industrial microbiology & biotechnology · 2015Article
- Structure-guided functional characterization of DUF1460 reveals a highly specific NlpC/P60 amidase family.Structure (London, England : 1993) · 2014Article
- Structures of a bifunctional cell wall hydrolase CwlT containing a novel bacterial lysozyme and an NlpC/P60 DL-endopeptidase.Journal of molecular biology · 2014Article
- Chemistry of the retinoid (visual) cycle.Chemical reviews · 2014Review
- Cloning, expression, purification, crystallization and preliminary crystallographic analysis of the putative NlpC/P60 endopeptidase, TTHA0266, from Thermus thermophilus HB8.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
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12 authors.
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Abstract
NlpC/P60 superfamily papain-like enzymes play important roles in all kingdoms of life. Two members of this superfamily, LRAT-like and YaeF/YiiX-like families, were predicted to contain a catalytic domain that is circularly permuted such that the catalytic cysteine is located near the C-terminus, instead of at the N-terminus. These permuted enzymes are widespread in virus, pathogenic bacteria, and eukaryotes. We determined the crystal structure of a member of the YaeF/YiiX-like family from Bacillus cereus in complex with lysine. The structure, which adopts a ligand-induced, "closed" conformation, confirms the circular permutation of catalytic residues. A comparative analysis of other related protein structures within the NlpC/P60 superfamily is presented. Permutated NlpC/P60 enzymes contain a similar conserved core and arrangement of catalytic residues, including a Cys/His-containing triad and an additional conserved tyrosine. More surprisingly, permuted enzymes have a hydrophobic S1 binding pocket that is distinct from previously characterized enzymes in the family, indicative of novel substrate specificity. Further analysis of a structural homolog, YiiX (PDB 2if6) identified a fatty acid in the conserved hydrophobic pocket, thus providing additional insights into possible function of these novel enzymes.
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