Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms.
EMBO J
; 20(21): 5813-21, 2001 Nov 01.
Article
en En
| MEDLINE
| ID: mdl-11689422
Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In contrast to the classical switch GTPases, a force-generating function has been suggested for dynamins. Here we report the 2.3 A crystal structure of the nucleotide-free and GDP-bound GTPase domain of Dictyostelium discoideum dynamin A. The GTPase domain is the most highly conserved region among dynamins. The globular structure contains the G-protein core fold, which is extended from a six-stranded beta-sheet to an eight-stranded one by a 55 amino acid insertion. This topologically unique insertion distinguishes dynamins from other subfamilies of GTP-binding proteins. An additional N-terminal helix interacts with the C-terminal helix of the GTPase domain, forming a hydrophobic groove, which could be occupied by C-terminal parts of dynamin not present in our construct. The lack of major conformational changes between the nucleotide-free and the GDP-bound state suggests that mechanochemical rearrangements in dynamin occur during GTP binding, GTP hydrolysis or phosphate release and are not linked to loss of GDP.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Modelos Moleculares
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Estructura Terciaria de Proteína
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Dinaminas
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GTP Fosfohidrolasas
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Guanosina Difosfato
Idioma:
En
Revista:
EMBO J
Año:
2001
Tipo del documento:
Article
País de afiliación:
Alemania
Pais de publicación:
Reino Unido