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The structure of the TOG-like domain of Drosophila melanogaster Mast/Orbit.

ABSTRACT: Mast/Orbit is a nonmotor microtubule-associated protein (MAP) present in Drosophila melanogaster that reportedly binds microtubules at the plus end and is essential for mitosis. Sequence analysis has shown that the N-terminal domain (Mast-M1) resembles TOG domains from the Dis1-TOG family of proteins and stands as a representative of one of the three subclasses of divergent TOG-like domains (TOGL1) that includes human CLASP1. The crystal structure of Mast-M1 has been determined at 2.0 Å resolution and provides the first detailed structural description of any TOG-like domain. The structure confirms that Mast-M1 adopts a similar fold to the previously described Dis1-TOG domains of microtubule-binding proteins. A comparison with three known TOG-domain structures from XMAP215/Dis1 family members exposes significant differences between Mast-M1 and other TOG-domain structures in key residues at the proposed tubulin-binding edge.

SUBMITTER: De la Mora-Rey T

PROVIDER: S-EPMC3702313 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature

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The structure of the TOG-like domain of Drosophila melanogaster Mast/Orbit.

De la Mora-Rey Teresa T Guenther Brian D BD Finzel Barry C BC

Acta crystallographica. Section F, Structural biology and crystallization communications 20130627 Pt 7

Mast/Orbit is a nonmotor microtubule-associated protein (MAP) present in Drosophila melanogaster that reportedly binds microtubules at the plus end and is essential for mitosis. Sequence analysis has shown that the N-terminal domain (Mast-M1) resembles TOG domains from the Dis1-TOG family of proteins and stands as a representative of one of the three subclasses of divergent TOG-like domains (TOGL1) that includes human CLASP1. The crystal structure of Mast-M1 has been determined at 2.0 Å resoluti ...[more]

PMID: 23832196

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