ArticleThe Journal of biological chemistry2012
Structural basis for activation of an integral membrane protease by lipopolysaccharide.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Lipopolysaccharide of theBiomolecules · 2021Review
- Review
- Review
- COVID-19: Review on latest available drugs and therapies against SARS-CoV-2. Coagulation and inflammation cross-talking.Virus research · 2020Review
- Role of Lipopolysaccharide in Protecting OmpT from Autoproteolysis during In Vitro Refolding.Biomolecules · 2020Article
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies.Communications biology · 2018Article
- Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Antimicrobial Peptide Conformation as a Structural Determinant of Omptin Protease Specificity.Journal of bacteriology · 2015Article
- Inhibition of outer membrane proteases of the omptin family by aprotinin.Infection and immunity · 2015Article
- The outer membrane protease PgtE of Salmonella enterica interferes with the alternative complement pathway by cleaving factors B and H.Frontiers in microbiology · 2015Article
- Article
- Article
- Catalytic site identification--a web server to identify catalytic site structural matches throughout PDB.Nucleic acids research · 2013Article
- RfaL is required for Yersinia pestis type III secretion and virulence.Infection and immunity · 2013Article
- Fibrinolytic and coagulative activities of Yersinia pestis.Frontiers in cellular and infection microbiology · 2013Review
- Yersinia infection tools-characterization of structure and function of adhesins.Frontiers in cellular and infection microbiology · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Omptins constitute a unique family of outer membrane proteases that are widespread in Enterobacteriaceae. The plasminogen activator (Pla) of Yersinia pestis is an omptin family member that is very important for development of both bubonic and pneumonic plague. The physiological function of Pla is to cleave (activate) human plasminogen to form the plasma protease plasmin. Uniquely, lipopolysaccharide (LPS) is essential for the catalytic activity of all omptins, including Pla. Why omptins require LPS for enzymatic activity is unknown. Here, we report the co-crystal structure of LPS-free Pla in complex with the activation loop peptide of human plasminogen, its natural substrate. The structure shows that in the absence of LPS, the peptide substrate binds deep within the active site groove and displaces the nucleophilic water molecule, providing an explanation for the dependence of omptins on LPS for enzymatic activity.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.