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Crystallization and preliminary X-ray crystallographic studies of a Lys49-phospholipase A{sub 2} homologue from Bothrops pirajai venom complexed with rosmarinic acid

Abstract

PrTX-I, a noncatalytic and myotoxic Lys49-phospholipase A{sub 2} from B. pirajai venom, was cocrystallized with the inhibitor rosmarinic acid from C. verbenacea. The crystals diffracted X-rays to 1.8 Å resolution and the structure was solved, indicating a remarkable electronic density for the ligand at the entrance to the hydrophobic channel. PrTX-I, a noncatalytic and myotoxic Lys49-phospholipase A{sub 2} from Bothrops pirajai venom, was crystallized in the presence of the inhibitor rosmarinic acid (RA). This is the active compound in the methanolic extract of Cordia verbenacea, a plant that is largely used in Brazilian folk medicine. The crystals diffracted X-rays to 1.8 Å resolution and the structure was solved by molecular-replacement techniques, showing electron density that corresponds to RA molecules at the entrance to the hydrophobic channel. The crystals belong to space group P2{sub 1}2{sub 1}2{sub 1}, indicating conformational changes in the structure after ligand binding: the crystals of all apo Lys49-phospholipase A{sub 2} structures belong to space group P3{sub 1}21, while the crystals of complexed structures belong to space groups P2{sub 1} or P2{sub 1}2{sub 1}2{sub 1}.
Authors:
Santos, Juliana I. dos; [1]  Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq (Brazil)]; Santos-Filho, Norival A.; Soares, Andreimar M.; [2]  Departamento de Análizes Clínicas, Toxicológicas e Bromatológicas, FCFRP, USP, Ribeirão Preto-SP (Brazil)]; Fontes, Marcos R. M.,; [1]  Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq (Brazil)]
  1. Departamento de Física e Biofísica, Instituto de Biociências, UNESP - Universidade Estadual Paulista, Botucatu-SP (Brazil)
  2. Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq (Brazil)
Publication Date:
Jun 01, 2010
Product Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 66; Journal Issue: Pt 6; Other Information: PMCID: PMC2882773; PMID: 20516603; PUBLISHER-ID: pu5296; OAI: oai:pubmedcentral.nih.gov:2882773; Copyright (c) International Union of Crystallography 2010; Country of input: International Atomic Energy Agency (IAEA)
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CONFORMATIONAL CHANGES; CRYSTALLIZATION; CRYSTALS; DENSITY; DRUGS; ELECTRON DENSITY; LIGANDS; MOLECULES; RESOLUTION; SPACE GROUPS
OSTI ID:
22367249
Country of Origin:
United Kingdom
Language:
English
Other Identifying Numbers:
Journal ID: ISSN 1744-3091; CODEN: ACSFCL; Other: PII: S1744309110013709; TRN: GB15$1001072581
Availability:
Available from http://dx.doi.org/10.1107/S1744309110013709; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2882773
Submitting Site:
INIS
Size:
page(s) 699-701
Announcement Date:
Jul 29, 2015

Citation Formats

Santos, Juliana I. dos, Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq (Brazil)], Santos-Filho, Norival A., Soares, Andreimar M., Departamento de Análizes Clínicas, Toxicológicas e Bromatológicas, FCFRP, USP, Ribeirão Preto-SP (Brazil)], Fontes, Marcos R. M.,, and Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq (Brazil)]. Crystallization and preliminary X-ray crystallographic studies of a Lys49-phospholipase A{sub 2} homologue from Bothrops pirajai venom complexed with rosmarinic acid. United Kingdom: N. p., 2010. Web. doi:10.1107/S1744309110013709.
Santos, Juliana I. dos, Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq (Brazil)], Santos-Filho, Norival A., Soares, Andreimar M., Departamento de Análizes Clínicas, Toxicológicas e Bromatológicas, FCFRP, USP, Ribeirão Preto-SP (Brazil)], Fontes, Marcos R. M.,, & Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq (Brazil)]. Crystallization and preliminary X-ray crystallographic studies of a Lys49-phospholipase A{sub 2} homologue from Bothrops pirajai venom complexed with rosmarinic acid. United Kingdom. doi:10.1107/S1744309110013709.
Santos, Juliana I. dos, Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq (Brazil)], Santos-Filho, Norival A., Soares, Andreimar M., Departamento de Análizes Clínicas, Toxicológicas e Bromatológicas, FCFRP, USP, Ribeirão Preto-SP (Brazil)], Fontes, Marcos R. M.,, and Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq (Brazil)]. 2010. "Crystallization and preliminary X-ray crystallographic studies of a Lys49-phospholipase A{sub 2} homologue from Bothrops pirajai venom complexed with rosmarinic acid." United Kingdom. doi:10.1107/S1744309110013709. https://www.osti.gov/servlets/purl/10.1107/S1744309110013709.
@misc{etde_22367249,
title = {Crystallization and preliminary X-ray crystallographic studies of a Lys49-phospholipase A{sub 2} homologue from Bothrops pirajai venom complexed with rosmarinic acid}
author = {Santos, Juliana I. dos, Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq (Brazil)], Santos-Filho, Norival A., Soares, Andreimar M., Departamento de Análizes Clínicas, Toxicológicas e Bromatológicas, FCFRP, USP, Ribeirão Preto-SP (Brazil)], Fontes, Marcos R. M.,, and Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq (Brazil)]}
abstractNote = {PrTX-I, a noncatalytic and myotoxic Lys49-phospholipase A{sub 2} from B. pirajai venom, was cocrystallized with the inhibitor rosmarinic acid from C. verbenacea. The crystals diffracted X-rays to 1.8 Å resolution and the structure was solved, indicating a remarkable electronic density for the ligand at the entrance to the hydrophobic channel. PrTX-I, a noncatalytic and myotoxic Lys49-phospholipase A{sub 2} from Bothrops pirajai venom, was crystallized in the presence of the inhibitor rosmarinic acid (RA). This is the active compound in the methanolic extract of Cordia verbenacea, a plant that is largely used in Brazilian folk medicine. The crystals diffracted X-rays to 1.8 Å resolution and the structure was solved by molecular-replacement techniques, showing electron density that corresponds to RA molecules at the entrance to the hydrophobic channel. The crystals belong to space group P2{sub 1}2{sub 1}2{sub 1}, indicating conformational changes in the structure after ligand binding: the crystals of all apo Lys49-phospholipase A{sub 2} structures belong to space group P3{sub 1}21, while the crystals of complexed structures belong to space groups P2{sub 1} or P2{sub 1}2{sub 1}2{sub 1}.}
doi = {10.1107/S1744309110013709}
journal = {Acta Crystallographica. Section F}
issue = {Pt 6}
volume = {66}
journal type = {AC}
place = {United Kingdom}
year = {2010}
month = {Jun}
}