ArticleThe protein journal2008
Homology modeling of hemagglutinin/protease [HA/P (vibriolysin)] from Vibrio cholerae: sequence comparision, residue interactions and molecular mechanism.
Article in The protein journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- DisarmingFrontiers in microbiology · 2019Article
- Accessory Toxins ofFrontiers in microbiology · 2018Review
- Vibrio cholerae hemagglutinin(HA)/protease: An extracellular metalloprotease with multiple pathogenic activities.Toxicon : official journal of the International Society on Toxinology · 2016Review
- Evidence for Cleavage of the Metalloprotease Vsm fromFrontiers in microbiology · 2016Article
- Mechanistic insights into elastin degradation by pseudolysin, the major virulence factor of the opportunistic pathogen Pseudomonas aeruginosa.Scientific reports · 2015Article
- Biofilm-degrading enzymes from Lysobacter gummosus.Virulence · 2014Article
- Highly sensitive quenched fluorescent substrate of Legionella major secretory protein (msp) based on its structural analysis.The Journal of biological chemistry · 2012Article
- Comparative analysis of binding affinities between styrene and mammalian CYP2E1 by bioinformatics approaches.Ecotoxicology (London, England) · 2011Article
- Genome pool strategy for structural coverage of protein families.Structure (London, England : 1993) · 2008Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vibrio cholerae produces a zinc-containing and calcium-stabilized soluble hemagglutinin/protease, which has been earlier shown to have the ability to cleave several physiologically important substrates including mucin, fibronectin and lactoferin. This study presents homology modeling of hemagglutinin/protease (vibriolysin) from Vibrio cholerae in the presence of inhibitor HPI [N-(1-carboxy-3-phenylpropyl)-phenylalanyl-alpha-aspargine]. The 3D structure was predicted based on its sequence homology with Pseudomonas aeruginosa elastase (PAE). Comparison of the 3D structures of PAE and HA/P reveals a remarkable similarity having a conserved alpha + beta domain. The inhibitor shows similar binding features as seen in other metalloproteases of M4 peptidase family. The study also highlights the key catalytic residues as well as the residues at the S1 and S1' binding sub-sites. The similarities between the two proteins provide support for the hypothesis that the two enzymes have similar three-dimensional structures and a common mechanism of action. The fact that both enzymes are secreted as zinc-containing proteases, led us to further hypothesize that they may play similar role in pathogenesis.
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Registered trials
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