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Structure-Function Relationship of a Novel PR-5 Protein with Antimicrobial Activity from Soy Hulls.

Identifieur interne : 000B25 ( Main/Exploration ); précédent : 000B24; suivant : 000B26

Structure-Function Relationship of a Novel PR-5 Protein with Antimicrobial Activity from Soy Hulls.

Auteurs : Chun Liu [République populaire de Chine] ; Fenfen Cheng [République populaire de Chine] ; Yingen Sun [République populaire de Chine] ; Hongyu Ma [République populaire de Chine] ; Xiaoquan Yang [République populaire de Chine]

Source :

RBID : pubmed:26753535

Descripteurs français

English descriptors

Abstract

An alkaline isoform of the PR-5 protein (designated GmOLPc) has been purified from soybean hulls and identified by MALDI-TOF/TOF-MS. GmOLPc effectively inhibited in vitro the growth of Phytophthora soja spore and Pseudomonas syringae pv glycinea. The antimicrobial activity of GmOLPc should be mainly ascribed to its high binding affinity with vesicles composed of DPPG, (1,3)-β-D-glucans, and weak endo-(1,3)-β-D-glucanase activity. From the 3D models, predicted by the homology modeling, GmOLPc contains an extended negatively charged cleft. The cleft was proved to be a prerequisite for endo-(1,3)-β-D-glucanase activity. Molecular docking revealed that the positioning of linear (1,3)-β-D-glucans in the cleft of GmOLPc allowed an interaction with Glu83 and Asp101 that were responsible for the hydrolytic cleavage of glucans. Interactions of GmOLPc with model membranes indicated that GmOLPc possesses good surface activity which could contribute to its antimicrobial activity, as proved by the behavior of perturbing the integrity of membranes through surface hydrophobic amino acid residues (Phe89 and Phe94).

DOI: 10.1021/acs.jafc.5b04771
PubMed: 26753535


Affiliations:


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Le document en format XML

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<div type="abstract" xml:lang="en">An alkaline isoform of the PR-5 protein (designated GmOLPc) has been purified from soybean hulls and identified by MALDI-TOF/TOF-MS. GmOLPc effectively inhibited in vitro the growth of Phytophthora soja spore and Pseudomonas syringae pv glycinea. The antimicrobial activity of GmOLPc should be mainly ascribed to its high binding affinity with vesicles composed of DPPG, (1,3)-β-D-glucans, and weak endo-(1,3)-β-D-glucanase activity. From the 3D models, predicted by the homology modeling, GmOLPc contains an extended negatively charged cleft. The cleft was proved to be a prerequisite for endo-(1,3)-β-D-glucanase activity. Molecular docking revealed that the positioning of linear (1,3)-β-D-glucans in the cleft of GmOLPc allowed an interaction with Glu83 and Asp101 that were responsible for the hydrolytic cleavage of glucans. Interactions of GmOLPc with model membranes indicated that GmOLPc possesses good surface activity which could contribute to its antimicrobial activity, as proved by the behavior of perturbing the integrity of membranes through surface hydrophobic amino acid residues (Phe89 and Phe94).</div>
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<name sortKey="Yang, Xiaoquan" sort="Yang, Xiaoquan" uniqKey="Yang X" first="Xiaoquan" last="Yang">Xiaoquan Yang</name>
<name sortKey="Yang, Xiaoquan" sort="Yang, Xiaoquan" uniqKey="Yang X" first="Xiaoquan" last="Yang">Xiaoquan Yang</name>
</country>
</tree>
</affiliations>
</record>

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