Insights on the structure and stability of Licanantase: a trimeric acid-stable coiled-coil lipoprotein from Acidithiobacillus thiooxidans
Author
dc.contributor.author
Abarca, Fernando
Author
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Gutiérrez Maldonado, Sebastián
Author
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Parada, Pilar
Author
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Martínez, Patricio
Author
dc.contributor.author
Maass Sepúlveda, Alejandro
Author
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Pérez Acle, Tomás
Admission date
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2015-08-12T15:02:34Z
Available date
dc.date.available
2015-08-12T15:02:34Z
Publication date
dc.date.issued
2014
Cita de ítem
dc.identifier.citation
PEERJ Volumen: 2 Número de artículo: e457, aug 5 2014
en_US
Identifier
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2167-8359
Identifier
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DOI: 10.7717/peerj.457
Identifier
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https://repositorio.uchile.cl/handle/2250/132630
General note
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Artículo de publicación ISI
en_US
Abstract
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Licanantase (Lic) is the major component of the secretome of Acidithiobacillus
thiooxidans when grown in elemental sulphur. When used as an additive, Lic improves
copper recovery frombioleaching processes. However, this recovery enhancement
is not fully understood. In this context, our aim is to predict the 3D structure of
Lic, to shed light on its structure-function relationships. Bioinformatics analyses on
the amino acid sequence of Lic showed a great similarity with Lpp, an Escherichia coli
Lipoprotein that can formstable trimers in solution. Lic and Lpp share the secretion
motif, intracellular processing and alpha helix structure, as well as the distribution of
hydrophobic residues in heptads forming a hydrophobic core, typical of coiled-coil
structures. Cross-linking experiments showed the presence of Lic trimers, supporting
our predictions. Taking the in vitro and in silico evidence as a whole, we propose that
the most probable structure for Lic is a trimeric coiled-coil. According to this prediction,
a suitable model for Lic was produced using the de novo algorithm “Rosetta
Fold-and-Dock”. To assess the structural stability of our model,Molecular Dynamics
(MD) and Replica Exchange MD simulations were performed using the structure of
Lpp and a 14-alanine Lpp mutant as controls, at both acidic and neutral pH. Our
results suggest that Lic was the most stable structure among the studied proteins in
both pH conditions. This increased stability can be explained by a higher number of
both intermonomer hydrophobic contacts and hydrogen bonds, key elements for the
stability of Lic’s secondary and tertiary structure
en_US
Patrocinador
dc.description.sponsorship
FCV
PFB16
FONDAP
CRG 15090007
Millennium Institute Centro Interdisciplinario de Neurociencias de Valparaiso
ICM-ECONOMIA P09-22-F
CIRIC INRIA-Chile
NLHPC
ECM-02
CONICYT