ArticleProtein science : a publication of the Protein Society2002
Breaking the singleton of germination protease.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 13 citations in OpenAlex.
- Article
- Fungal proteases and their pathophysiological effects.Mycopathologia · 2011Review
- Site-directed mutagenesis and structural studies suggest that the germination protease, GPR, in spores of Bacillus species is an atypical aspartic acid protease.Journal of bacteriology · 2005Article
- The P5 protein from bacteriophage phi-6 is a distant homolog of lytic transglycosylases.Protein science : a publication of the Protein Society · 2005Article
- Presence and expression of hydrogenase specific C-terminal endopeptidases in cyanobacteria.BMC microbiology · 2003Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Germination protease (GPR) plays an important role in the germination of spores of Bacillus and Clostridium species. A few very similar GPRs form a singleton group without significant sequence similarities to any other proteins. Their active site locations and catalytic mechanisms are unclear, despite the recent 3-D structure determination of Bacillus megaterium GPR. Using structural comparison and sequence analysis, we show that GPR is homologous to bacterial hydrogenase maturation protease (HybD). HybD's activity relies on the recognition and binding of metal ions in Ni-Fe hydrogenase, its substrate. Two highly conserved motifs are shared among GPRs, hydrogenase maturation proteases, and another group of hypothetical proteins. Conservation of two acidic residues in all these homologs indicates that metal binding is important for their function. Our analysis helps localize the active site of GPRs and provides insight into the catalytic mechanisms of a superfamily of putative metal-regulated proteases.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.