ArticleBioMed research international2013
In silico determination and validation of baumannii acinetobactin utilization a structure and ligand binding site.
Article in BioMed research international, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Bacteriophages targetingFrontiers in microbiology · 2026Review
- In Silico Development of a Chimeric Multi-Epitope Vaccine TargetingPharmaceuticals (Basel, Switzerland) · 2025Article
- Cloning, Characterization, Expression Analysis, and Agglutination Studies of Novel Gene Encoding β-D-Galactose, N-Acetyl-D-Glucosamine and Lactose-Binding Lectin from Rice Bean (Vigna umbellata).Molecular biotechnology · 2022Article
- Subunit vaccines forFrontiers in immunology · 2022Review
- In silico Structural, Functional and Phylogenetic Analyses of cellulase from Ruminococcus albus.Journal, genetic engineering & biotechnology · 2021Article
- Distribution of virulence-associated genes and antimicrobial susceptibility in clinicalOncotarget · 2018Article
- Antibiotic Resistance Determinant-Focused Acinetobacter baumannii Vaccine Designed Using Reverse Vaccinology.International journal of molecular sciences · 2017Article
- Immunogenicity of Cork and Loop Domains of RecombinantAvicenna journal of medical biotechnologyArticle
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acinetobacter baumannii is a deadly nosocomial pathogen. Iron is an essential element for the pathogen. Under iron-restricted conditions, the bacterium expresses iron-regulated outer membrane proteins (IROMPs). Baumannii acinetobactin utilization (BauA) is the most important member of IROMPs in A. baumannii. Determination of its tertiary structure could help deduction of its functions and its interactions with ligands. The present study unveils BauA 3D structure via in silico approaches. Apart from ab initio, other rational methods such as homology modeling and threading were invoked to achieve the purpose. For homology modeling, BLAST was run on the sequence in order to find the best template. The template was then served to model the 3D structure. All the models built were evaluated qualitatively. The best model predicted by LOMETS was selected for analyses. Refinement of 3D structure as well as determination of its clefts and ligand binding sites was carried out on the structure. In contrast to the typical trimeric arrangement found in porins, BauA is monomeric. The barrel is formed by 22 antiparallel transmembrane β -strands. There are short periplasmic turns and longer surface-located loops. An N-terminal domain referred to either as the cork, the plug, or the hatch domain occludes the β -barrel.
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Registered trials
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