Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates

Katiuscia Pagano, Francesco Bemporad, Federico Fogolari, Gennaro Esposito, Paolo Viglino, Fabrizio Chiti, Alessandra Corazza

Research output: Contribution to journalArticle

Abstract

It has previously been shown that the acylphosphatase from Sulfolobus solfataricus is capable of forming amyloid-like aggregates under conditions in which the native structure is maintained and via the transient formation of native-like aggregates. Based on the previously determined NMR structure of the native protein, showing a ferredoxin-like fold and the peculiar presence of an unstructured N-terminal segment, we show here, at a molecular level using NMR spectroscopy, that indeed S. solfataricus acylphosphatase remains in a native-like conformation when placed in aggregating conditions and that such a native-like structure persists when the protein forms the initial aggregates, at least within the low molecular weight species. The analysis carried out under different solution conditions, based on the measurement of the combined 1H and 15N chemical shifts and hydrogen/deuterium exchange rates, enabled the most significant conformational changes to be monitored upon transfer of the monomeric state into aggregating conditions and upon formation of the initial native-like aggregates. Important increases of the hydrogen/deuterium exchange rates throughout the native protein, accompanied by small and localized structural changes, in the monomeric protein were observed. The results also allow the identification of the intermolecular interaction regions within the native-like aggregates, that involve, in particular, the N-terminal unstructured segment, the apical region including strands S4 and S5 with the connecting loop, and the opposite active site.

Original languageEnglish (US)
Pages (from-to)14689-14700
Number of pages12
JournalJournal of Biological Chemistry
Volume285
Issue number19
DOIs
StatePublished - May 7 2010

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Sulfolobus solfataricus
Deuterium
Hydrogen
Proteins
Ferredoxins
Amyloid
Chemical shift
Catalytic Domain
Magnetic Resonance Spectroscopy
Molecular Weight
Nuclear magnetic resonance spectroscopy
Conformations
Molecular weight
Nuclear magnetic resonance
acylphosphatase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates. / Pagano, Katiuscia; Bemporad, Francesco; Fogolari, Federico; Esposito, Gennaro; Viglino, Paolo; Chiti, Fabrizio; Corazza, Alessandra.

In: Journal of Biological Chemistry, Vol. 285, No. 19, 07.05.2010, p. 14689-14700.

Research output: Contribution to journalArticle

Pagano, Katiuscia ; Bemporad, Francesco ; Fogolari, Federico ; Esposito, Gennaro ; Viglino, Paolo ; Chiti, Fabrizio ; Corazza, Alessandra. / Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates. In: Journal of Biological Chemistry. 2010 ; Vol. 285, No. 19. pp. 14689-14700.
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