ArticleJournal of computer-aided molecular design2012
Structural prediction of a novel chitinase from the psychrophilic Glaciozyma antarctica PI12 and an analysis of its structural properties and function.
Article in Journal of computer-aided molecular design, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 44 citations in OpenAlex.
- Yeasts associated with microalgal cultures in marine environments: ecological roles and biotechnological potential.FEMS yeast research · 2026Review
- Structural Insights into Cold-Active Lipase from Glaciozyma antarctica PI12: Alphafold2 Prediction and Molecular Dynamics Simulation.Journal of molecular evolution · 2024Article
- Genomic signatures of cold adaptation in the family Colwelliaceae.Extremophiles : life under extreme conditions · 2024Article
- Extracellular Enzymatic Activities of Oceanic Pelagic Fungal Strains and the Influence of Temperature.Journal of fungi (Basel, Switzerland) · 2022Article
- Cold Adaptation Strategies and the Potential of Psychrophilic Enzymes from the Antarctic Yeast,Journal of fungi (Basel, Switzerland) · 2021Review
- Diversity, Ecological Role and Biotechnological Potential of Antarctic Marine Fungi.Journal of fungi (Basel, Switzerland) · 2021Review
- Comparative modelling studies of fruit bromelain using molecular dynamics simulation.Journal of molecular modeling · 2020Article
- Extremophile - An Adaptive Strategy for Extreme Conditions and Applications.Current genomics · 2020Review
- Fungal and bacterial diversity of Svalbard subglacial ice.Scientific reports · 2019Article
- A Novel Cold-Adapted and Salt-Tolerant RNase R from Antarctic Sea-Ice BacteriumMolecules (Basel, Switzerland) · 2019Article
- Article
- Structural and functional insights into TRiC chaperonin from a psychrophilic yeast, Glaciozyma antarctica.Cell stress & chaperones · 2019Article
- Darkening of the Greenland Ice Sheet: Fungal Abundance and Diversity Are Associated With Algal Bloom.Frontiers in microbiology · 2019Article
- Biochemical and structural characterization of a novel cold-active esterase-like protein from the psychrophilic yeast Glaciozyma antarctica.Extremophiles : life under extreme conditions · 2018Article
- Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Structural and functional analysis of a novel psychrophilic β-mannanase from Glaciozyma antarctica PI12.Journal of computer-aided molecular design · 2014Article
- Sequence and structural investigation of a novel psychrophilic α-amylase from Glaciozyma antarctica PI12 for cold-adaptation analysis.Journal of molecular modeling · 2013Article
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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
The structure of psychrophilic chitinase (CHI II) from Glaciozyma antarctica PI12 has yet to be studied in detail. Due to its low sequence identity (<30 %), the structural prediction of CHI II is a challenge. A 3D model of CHI II was built by first using a threading approach to search for a suitable template and to generate an optimum target-template alignment, followed by model building using MODELLER9v7. Analysis of the catalytic insertion domain structure in CHI II revealed an increase in the number of aromatic residues and longer loops compared to mesophilic and thermophilic chitinases. A molecular dynamics simulation was used to examine the stability of the CHI II structure at 273, 288 and 300 K. Structural analysis of the substrate-binding cleft revealed a few exposed aromatic residues. Substitutions of certain amino acids in the surface and loop regions of CHI II conferred an increased flexibility to the enzyme, allowing for an adaptation to cold temperatures. A substrate binding comparison of CHI II with the mesophilic chitinase from Coccidioides immitis, 1D2K, suggested that the psychrophilic adaptation and catalytic activity at low temperatures were achieved through a reduction in the number of salt bridges, fewer hydrogen bonds and an increase in the exposure of the hydrophobic side chains to the solvent.
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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.