Oct 2026· Acta Crystallographica Section F Structural Biology Communications· 0 citations
Medicine
TL;DR
Structural features suggest that the Methylomonas protein that is identified may act as a BLF1-like deamidase but against a currently unknown target, and that other bacterial proteins with similar sequence fingerprints could play important roles in broader bacterial biology.
Biochemically characterizes Rv1063c as a medium-chain-specific esterase encoded by a protein homologous to the patatin superfamily as a medium-chain-specific esterase encoded by a protein homologous to the patatin superfamily.
Yuming Song, Song-Song Dong, Ru-Meng Zhai et al.· Frontiers in Microbiology· 0 citations
The authors' bioinformatic analyses expand the repertoire of auxiliary metabolic genes in Phycodnaviridae by identifying a conserved heme degradation pathway, non-canonical vHMOX1/PcyA targeting and structural rearrangements surrounding the catalytic sites of viral HMOX1.
Steven Zehnacker, S. Caffarri, G. Blanc et al.· bioRxiv· 0 citations
It is common for bacteriophages to encode proteins that are strongly inhibitory to growth of the bacterial host, and about 10% of mycobacteriophage-encoded proteins have this property. Adephagia is a Cluster K1 mycobacteriophage and prior cloning and expression of 66 Adephagia non-structural genes identified 14 that ar...
Michael J. Lauer, K. Freeman, Da Jiang et al.· bioRxiv· 0 citations
NMR data, in combination with enzymatic assays using active variants confirmed differences in the active, apo states of these enzymes, and provided additional atomic detail regarding the importance of the P94 residue in saSrtA substrate recognition.
Erich G. Walkenhauer, Noah Cox-Tigre, M. Chaubey et al.· bioRxiv· 0 citations
Methanogenic archaea harbor diverse enzymes that support their survival in extreme environments and play key roles in global carbon cycling. The C39 peptidase family, known for cleaving peptide substrates, now gains functional expansion through A0A126R2S0, a novel enzyme that shares structural homology with C39 peptida...
The RNase-H fold is an ancient protein fold found in diverse nucleases that is characterised by a conserved structural core (five β strands and ⍺ helices), canonical DDE/D catalytic residues and catalytic mechanism. This study focuses on the evolutionary conservation of the RNaseH-like domain in the transposase-derived...
Aditi Saha, S. Majumdar· bioRxiv· 0 citations
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