ArticleActa crystallographica. Section F, Structural biology communications2016
Structure of a thermostable serralysin from Serratia sp. FS14 at 1.1 Å resolution.
Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 26 citations in OpenAlex.
- Bioconjugation of Serratiopeptidase with Titanium Oxide Nanoparticles: Improving Stability and Antibacterial Properties.Journal of functional biomaterials · 2024Article
- Scale-Up of the Fermentation Process for the Production and Purification of Serratiopeptidase Using Silkworm Pupae as a Substrate.Methods and protocols · 2024Article
- Purification and characterization of thermoactive serratiopeptidase from Serratia marcescens AD-W2.AMB Express · 2021Article
- Production and Expression Optimization of Heterologous Serratiopeptidase.Iranian journal of public health · 2020Article
- System Approach for Building of Calcium-Binding Sites in Proteins.Biomolecules · 2020Article
- Review
- Purification, characterization, and structural elucidation of serralysin-like alkaline metalloprotease from a novel source.Journal, genetic engineering & biotechnology · 2019Article
- Serralysin family metalloproteases protects Serratia marcescens from predation by the predatory bacteria Micavibrio aeruginosavorus.Scientific reports · 2018Article
- Production, purification and characterization of fibrinolytic enzyme from Serratia sp. KG-2-1 using optimized media.3 Biotech · 2017Article
- Myroilysin Is a New Bacterial Member of the M12A Family of Metzincin Metallopeptidases and Is Activated by a Cysteine Switch Mechanism.The Journal of biological chemistry · 2017Article
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4 authors at 1 institution in 1 country.
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Abstract
Serralysin is a well studied metalloprotease, and typical serralysins are not thermostable. The serralysin isolated from Serratia sp. FS14 was found to be thermostable, and in order to reveal the mechanism responsible for its thermostability, the crystal structure of serralysin from Serratia sp. FS14 was solved to a crystallographic R factor of 0.1619 at 1.10 Å resolution. Similar to its homologues, it mainly consists of two domains: an N-terminal catalytic domain and a `parallel β-roll' C-terminal domain. Comparative studies show that the shape of the catalytic active-site cavity is more open owing to the 189-198 loop, with a short 310-helix protruding further from the molecular surface, and that the β-sheets comprising the `parallel β-roll' are longer than those in its homologues. The formation of hydrogen bonds from one of the nonconserved residues (Asn200) to Lys27 may contribute to the thermostability.
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