Crystal Structure of a Type IV Pilus Assembly ATPase: Insights into the Molecular Mechanism of PilB from Thermus thermophilus.
Structure
; 24(11): 1886-1897, 2016 11 01.
Article
en En
| MEDLINE
| ID: mdl-27667690
ABSTRACT
Type IV pili (T4P) mediate bacterial motility and virulence. The PilB/GspE family ATPases power the assembly of T4P and type 2 secretion systems. We determined the structure of the ATPase region of PilB (PilBATP) in complex with ATPγS to provide a model of a T4P assembly ATPase and a view of a PilB/GspE family hexamer at better than 3-Šresolution. Spatial positioning and conformations of the protomers suggest a mechanism of force generation. All six PilBATP protomers contain bound ATPγS. Two protomers form a closed conformation poised for ATP hydrolysis. The other four molecules assume an open conformation but separate into two pairs with distinct active-site accessibilities. We propose that one pair represents the post-hydrolysis phase while the other pair appears poised for ADP/ATP exchange. Collectively, the data suggest that T4P assembly is powered by coordinating concurrent substrate binding with ATP hydrolysis across the PilB hexamer.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Oxidorreductasas
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Proteínas Bacterianas
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Adenosina Trifosfato
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Thermus thermophilus
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Fimbrias Bacterianas
Idioma:
En
Año:
2016
Tipo del documento:
Article