Molecular and structural insights into an asymmetric proteolytic complex (ClpP1P2) from Mycobacterium smegmatis.
Sci Rep
; 9(1): 18019, 2019 12 02.
Article
em En
| MEDLINE
| ID: mdl-31792243
ABSTRACT
The ClpP protease is found in all kingdoms of life, from bacteria to humans. In general, this protease forms a homo-oligomeric complex composed of 14 identical subunits, which associates with its cognate ATPase in a symmetrical manner. Here we show that, in contrast to this general architecture, the Clp protease from Mycobacterium smegmatis (Msm) forms an asymmetric hetero-oligomeric complex ClpP1P2, which only associates with its cognate ATPase through the ClpP2 ring. Our structural and functional characterisation of this complex demonstrates that asymmetric docking of the ATPase component is controlled by both the composition of the ClpP1 hydrophobic pocket (Hp) and the presence of a unique C-terminal extension in ClpP1 that guards this Hp. Our structural analysis of MsmClpP1 also revealed openings in the side-walls of the inactive tetradecamer, which may represent sites for product egress.
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
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Mycobacterium smegmatis
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Subunidades Proteicas
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Endopeptidase Clp
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Multimerização Proteica
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article