4G3A

Crystal Structure of MAST/Orbit N-terminal domain

Summary for 4G3A

• Entry DOI: 10.2210/pdb4g3a/pdb
• Descriptor: CLIP-associating protein, GLYCEROL (3 entities in total)
• Functional Keywords: tog domain, heat repeat, map protein, microtubule, cell cycle
• Biological source: Drosophila melanogaster (Fruit fly)
• Cellular location: Cytoplasm, cytoskeleton: Q9NBD7
• Total number of polymer chains: 2
• Total formula weight: 55135.21

Authors

De la Mora-Rey, T. (deposition date: 2012-07-13, release date: 2013-07-17, Last modification date: 2024-11-20)

Primary citation

De la Mora-Rey, T.,Guenther, B.D.,Finzel, B.C.
The structure of the TOG-like domain of Drosophila melanogaster Mast/Orbit.
Acta Crystallogr.,Sect.F, 69:723-729, 2013

PubMed 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.

PubMed: 23832196
DOI: 10.1107/S1744309113015182

Experimental method

X-RAY DIFFRACTION (1.994 Å)