Cargando…

The Sequence and Three-Dimensional Structure Characterization of Snake Venom Phospholipases B

Snake venom phospholipases B (SVPLBs) are the least studied enzymes. They constitute about 1% of Bothrops crude venoms, however, in other snake venoms, it is present in less than 1%. These enzymes are considered the most potent hemolytic agent in the venom. Currently, no structural information is av...

Descripción completa

Detalles Bibliográficos
Autores principales: Ullah, Anwar, Masood, Rehana
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7419708/
https://www.ncbi.nlm.nih.gov/pubmed/32850964
http://dx.doi.org/10.3389/fmolb.2020.00175
_version_ 1783569942829858816
author Ullah, Anwar
Masood, Rehana
author_facet Ullah, Anwar
Masood, Rehana
author_sort Ullah, Anwar
collection PubMed
description Snake venom phospholipases B (SVPLBs) are the least studied enzymes. They constitute about 1% of Bothrops crude venoms, however, in other snake venoms, it is present in less than 1%. These enzymes are considered the most potent hemolytic agent in the venom. Currently, no structural information is available about these enzymes from snake venom. To better understand its three-dimensional structure and mechanisms of envenomation, the current work describes the first model-based structure report of this enzyme from Bothrops moojeni venom named as B. moojeni phospholipase B (PLB_Bm). The structure model of PLB_Bm was generated using model building software like I-TESSER, MODELLER 9v19, and Swiss-Model. The build PLB_Bm model was validated using validation tools (PROCHECK, ERRAT, and Verif3D). The analysis of the PLB_Bm modeled structure indicates that it contains 491 amino acid residues that form a well-defined four-layer αββα sandwich core and has a typical fold of the N-terminal nucleophile aminohydrolase (Ntn-hydrolase). The overall structure of PLB_Bm contains 18 β-strands and 17 α-helices with many connecting loops. The structure divides into two chains (A and B) after maturation. The A chain is smaller and contains 207 amino acid residues, whereas the B chain is larger and contains 266 amino acid residues. The sequence and structural comparison among homologous snake venom, bacterial, and mammals PLBs indicate that differences in the length and sequence composition may confer variable substrate specificity to these enzymes. Moreover, the surface charge distribution, average volume, and depth of the active site cavity also vary in these enzymes. The present work will provide more information about the structure–function relationship and mechanism of action of these enzymes in snakebite envenomation.
format Online
Article
Text
id pubmed-7419708
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher Frontiers Media S.A.
record_format MEDLINE/PubMed
spelling pubmed-74197082020-08-25 The Sequence and Three-Dimensional Structure Characterization of Snake Venom Phospholipases B Ullah, Anwar Masood, Rehana Front Mol Biosci Molecular Biosciences Snake venom phospholipases B (SVPLBs) are the least studied enzymes. They constitute about 1% of Bothrops crude venoms, however, in other snake venoms, it is present in less than 1%. These enzymes are considered the most potent hemolytic agent in the venom. Currently, no structural information is available about these enzymes from snake venom. To better understand its three-dimensional structure and mechanisms of envenomation, the current work describes the first model-based structure report of this enzyme from Bothrops moojeni venom named as B. moojeni phospholipase B (PLB_Bm). The structure model of PLB_Bm was generated using model building software like I-TESSER, MODELLER 9v19, and Swiss-Model. The build PLB_Bm model was validated using validation tools (PROCHECK, ERRAT, and Verif3D). The analysis of the PLB_Bm modeled structure indicates that it contains 491 amino acid residues that form a well-defined four-layer αββα sandwich core and has a typical fold of the N-terminal nucleophile aminohydrolase (Ntn-hydrolase). The overall structure of PLB_Bm contains 18 β-strands and 17 α-helices with many connecting loops. The structure divides into two chains (A and B) after maturation. The A chain is smaller and contains 207 amino acid residues, whereas the B chain is larger and contains 266 amino acid residues. The sequence and structural comparison among homologous snake venom, bacterial, and mammals PLBs indicate that differences in the length and sequence composition may confer variable substrate specificity to these enzymes. Moreover, the surface charge distribution, average volume, and depth of the active site cavity also vary in these enzymes. The present work will provide more information about the structure–function relationship and mechanism of action of these enzymes in snakebite envenomation. Frontiers Media S.A. 2020-08-05 /pmc/articles/PMC7419708/ /pubmed/32850964 http://dx.doi.org/10.3389/fmolb.2020.00175 Text en Copyright © 2020 Ullah and Masood. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Molecular Biosciences
Ullah, Anwar
Masood, Rehana
The Sequence and Three-Dimensional Structure Characterization of Snake Venom Phospholipases B
title The Sequence and Three-Dimensional Structure Characterization of Snake Venom Phospholipases B
title_full The Sequence and Three-Dimensional Structure Characterization of Snake Venom Phospholipases B
title_fullStr The Sequence and Three-Dimensional Structure Characterization of Snake Venom Phospholipases B
title_full_unstemmed The Sequence and Three-Dimensional Structure Characterization of Snake Venom Phospholipases B
title_short The Sequence and Three-Dimensional Structure Characterization of Snake Venom Phospholipases B
title_sort sequence and three-dimensional structure characterization of snake venom phospholipases b
topic Molecular Biosciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7419708/
https://www.ncbi.nlm.nih.gov/pubmed/32850964
http://dx.doi.org/10.3389/fmolb.2020.00175
work_keys_str_mv AT ullahanwar thesequenceandthreedimensionalstructurecharacterizationofsnakevenomphospholipasesb
AT masoodrehana thesequenceandthreedimensionalstructurecharacterizationofsnakevenomphospholipasesb
AT ullahanwar sequenceandthreedimensionalstructurecharacterizationofsnakevenomphospholipasesb
AT masoodrehana sequenceandthreedimensionalstructurecharacterizationofsnakevenomphospholipasesb