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

Teresa De La Mora-Rey, Brian D. Guenther, Barry C. Finzel

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)723-729
Number of pages7
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number7
DOIs
StatePublished - Jul 2013

Bibliographical note

Copyright:
Copyright 2013 Elsevier B.V., All rights reserved.

Keywords

  • CLASP
  • Dis1-TOG domain
  • TOG-like domains
  • XMAP215/Dis1
  • microtubules

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