Homology modeling of an antifungal metabolite plipastatin synthase from the Bacillus subtilis 168

Lipopeptides have a widespread role in different pathways of Bacillus subtilis; they can act as antagonists, spreader and immunostimulators. Plipastatin, an antifungal antibiotic, is one of the most important lipopeptide nonribosomly produced by Bacillus subtilis. Plipastatin has strong fungitoxic a...

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Main Authors:	Batool, Maria, Khalid, Mohammad Hassan, Hassan, Muhammad Nadeem, Fauzia Yusuf, Hafeez
Format:	Online
Language:	English
Published:	Biomedical Informatics 2011
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3280437/

id	pubmed-3280437
recordtype	oai_dc
spelling	pubmed-32804372012-02-17 Homology modeling of an antifungal metabolite plipastatin synthase from the Bacillus subtilis 168 Batool, Maria Khalid, Mohammad Hassan Hassan, Muhammad Nadeem Fauzia Yusuf, Hafeez Hypothesis Lipopeptides have a widespread role in different pathways of Bacillus subtilis; they can act as antagonists, spreader and immunostimulators. Plipastatin, an antifungal antibiotic, is one of the most important lipopeptide nonribosomly produced by Bacillus subtilis. Plipastatin has strong fungitoxic activity and involve in inhibition of phospholipase A2 and biofilm formation. For better understanding of the molecule and pathway by which lipopeptide plipastatin is synthesized, we present a computationally predicted structure of plipastatin using homology modeling. Primary and secondary structure analysis suggested that ppsD is a hydrophilic protein containing a significant proportion of alpha helices, and subcellular localization predictions suggested it is a cytoplasmic protein. The tertiary structure of protein (plipastatin synthase subunit D) was predicted by homology modeling. The results suggest a flexible structure which is also an important characteristic of active enzymes enabling them to bind various cofactors and substrates for proper functioning. Validation of 3D structure was done using Ramachandran plot ProsA-web and QMEAN score.This predicted information will help in better understanding of mechanisms underlying plipastatin synthase subunit D synthesis. Plipastatin can be used as an inhibitor of various fungal diseases in plants. Biomedical Informatics 2011-12-21 /pmc/articles/PMC3280437/ /pubmed/22347779 Text en © 2011 Biomedical Informatics This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Batool, Maria Khalid, Mohammad Hassan Hassan, Muhammad Nadeem Fauzia Yusuf, Hafeez
spellingShingle	Batool, Maria Khalid, Mohammad Hassan Hassan, Muhammad Nadeem Fauzia Yusuf, Hafeez Homology modeling of an antifungal metabolite plipastatin synthase from the Bacillus subtilis 168
author_facet	Batool, Maria Khalid, Mohammad Hassan Hassan, Muhammad Nadeem Fauzia Yusuf, Hafeez
author_sort	Batool, Maria
title	Homology modeling of an antifungal metabolite plipastatin synthase from the Bacillus subtilis 168
title_short	Homology modeling of an antifungal metabolite plipastatin synthase from the Bacillus subtilis 168
title_full	Homology modeling of an antifungal metabolite plipastatin synthase from the Bacillus subtilis 168
title_fullStr	Homology modeling of an antifungal metabolite plipastatin synthase from the Bacillus subtilis 168
title_full_unstemmed	Homology modeling of an antifungal metabolite plipastatin synthase from the Bacillus subtilis 168
title_sort	homology modeling of an antifungal metabolite plipastatin synthase from the bacillus subtilis 168
description	Lipopeptides have a widespread role in different pathways of Bacillus subtilis; they can act as antagonists, spreader and immunostimulators. Plipastatin, an antifungal antibiotic, is one of the most important lipopeptide nonribosomly produced by Bacillus subtilis. Plipastatin has strong fungitoxic activity and involve in inhibition of phospholipase A2 and biofilm formation. For better understanding of the molecule and pathway by which lipopeptide plipastatin is synthesized, we present a computationally predicted structure of plipastatin using homology modeling. Primary and secondary structure analysis suggested that ppsD is a hydrophilic protein containing a significant proportion of alpha helices, and subcellular localization predictions suggested it is a cytoplasmic protein. The tertiary structure of protein (plipastatin synthase subunit D) was predicted by homology modeling. The results suggest a flexible structure which is also an important characteristic of active enzymes enabling them to bind various cofactors and substrates for proper functioning. Validation of 3D structure was done using Ramachandran plot ProsA-web and QMEAN score.This predicted information will help in better understanding of mechanisms underlying plipastatin synthase subunit D synthesis. Plipastatin can be used as an inhibitor of various fungal diseases in plants.
publisher	Biomedical Informatics
publishDate	2011
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3280437/
_version_	1611506373182357504

Homology modeling of an antifungal metabolite plipastatin synthase from the Bacillus subtilis 168

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