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Three-Dimensional Structure of Arabidopsis thaliana Lipase Predicted by Homology Modeling Method.

Messaoudi A, Belguith H, Ben Hamida J - Evol. Bioinform. Online (2011)

Bottom Line: By contrast, very little is known about plant lipases.In this investigation, a homology model of Arabidopsis thaliana lipase (NP_179126) was constructed using a human gastric lipase (PDB ID: 1HLG), as a template for model building.Natural substrates: tributyrin, trioctanoin and triolen were docked into the model to investigate ligand-substrate interaction.

View Article: PubMed Central - PubMed

Affiliation: Unité de Protéomie Fonctionnelle and Biopréservation Alimentaire, Institut Supérieur des Sciences Biologiques Appliquées de Tunis, Université Tunis El Manar, Tunisie.

ABSTRACT
Triacylglycerol lipases have been thoroughly characterized in mammals and microorganisms. By contrast, very little is known about plant lipases. In this investigation, a homology model of Arabidopsis thaliana lipase (NP_179126) was constructed using a human gastric lipase (PDB ID: 1HLG), as a template for model building. This model was then assessed for stereochemical quality and side chain environment. Natural substrates: tributyrin, trioctanoin and triolen were docked into the model to investigate ligand-substrate interaction.

No MeSH data available.


Three-dimensional representation of substrates (A), tributyrin (B), trioctanoin and (C) triolen in the Arabidopsis thaliana lipase model active site after docking. For clarity purpose residues and ligands are shown in wireframe and stick form respectively.
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f5-ebo-7-2011-099: Three-dimensional representation of substrates (A), tributyrin (B), trioctanoin and (C) triolen in the Arabidopsis thaliana lipase model active site after docking. For clarity purpose residues and ligands are shown in wireframe and stick form respectively.

Mentions: Figure 5 shows that triolein does not bind the lipase at the same site as tributyrin and trioctanoin. In addition, the catalytic active site, serine S166, is not involved in the binding site, this result confirms that the lid domain which covers the active site is not accessible to solvent.


Three-Dimensional Structure of Arabidopsis thaliana Lipase Predicted by Homology Modeling Method.

Messaoudi A, Belguith H, Ben Hamida J - Evol. Bioinform. Online (2011)

Three-dimensional representation of substrates (A), tributyrin (B), trioctanoin and (C) triolen in the Arabidopsis thaliana lipase model active site after docking. For clarity purpose residues and ligands are shown in wireframe and stick form respectively.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3140413&req=5

f5-ebo-7-2011-099: Three-dimensional representation of substrates (A), tributyrin (B), trioctanoin and (C) triolen in the Arabidopsis thaliana lipase model active site after docking. For clarity purpose residues and ligands are shown in wireframe and stick form respectively.
Mentions: Figure 5 shows that triolein does not bind the lipase at the same site as tributyrin and trioctanoin. In addition, the catalytic active site, serine S166, is not involved in the binding site, this result confirms that the lid domain which covers the active site is not accessible to solvent.

Bottom Line: By contrast, very little is known about plant lipases.In this investigation, a homology model of Arabidopsis thaliana lipase (NP_179126) was constructed using a human gastric lipase (PDB ID: 1HLG), as a template for model building.Natural substrates: tributyrin, trioctanoin and triolen were docked into the model to investigate ligand-substrate interaction.

View Article: PubMed Central - PubMed

Affiliation: Unité de Protéomie Fonctionnelle and Biopréservation Alimentaire, Institut Supérieur des Sciences Biologiques Appliquées de Tunis, Université Tunis El Manar, Tunisie.

ABSTRACT
Triacylglycerol lipases have been thoroughly characterized in mammals and microorganisms. By contrast, very little is known about plant lipases. In this investigation, a homology model of Arabidopsis thaliana lipase (NP_179126) was constructed using a human gastric lipase (PDB ID: 1HLG), as a template for model building. This model was then assessed for stereochemical quality and side chain environment. Natural substrates: tributyrin, trioctanoin and triolen were docked into the model to investigate ligand-substrate interaction.

No MeSH data available.