1FFX

TUBULIN:STATHMIN-LIKE DOMAIN COMPLEX

Summary for 1FFX

• Entry DOI: 10.2210/pdb1ffx/pdb
• Descriptor: PROTEIN (TUBULIN), PROTEIN (STATHMIN-LIKE DOMAIN OF RB3), GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: alpha-tubulin, beta-tubulin, stathmin, microtubule, tubulin, structural protein
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cytoplasm, cytoskeleton: P02550 P02554
• Total number of polymer chains: 5
• Total formula weight: 209753.39

Authors

Gigant, B.,Martin-Barbey, C.,Knossow, M. (deposition date: 2000-07-26, release date: 2000-09-27, Last modification date: 2023-08-09)

Primary citation

Gigant, B.,Curmi, P.A.,Martin-Barbey, C.,Charbaut, E.,Lachkar, S.,Lebeau, L.,Siavoshian, S.,Sobel, A.,Knossow, M.
The 4 A X-ray structure of a tubulin:stathmin-like domain complex.
Cell(Cambridge,Mass.), 102:809-816, 2000

PubMed Abstract: Phosphoproteins of the stathmin family interact with the alphabeta tubulin heterodimer (tubulin) and hence interfere with microtubule dynamics. The structure of the complex of GDP-tubulin with the stathmin-like domain of the neural protein RB3 reveals a head-to-tail assembly of two tubulins with a 91-residue RB3 alpha helix in which each copy of an internal duplicated sequence interacts with a different tubulin. As a result of the relative orientations adopted by tubulins and by their alpha and beta subunits, the tubulin:RB3 complex forms a curved structure. The RB3 helix thus most likely prevents incorporation of tubulin into microtubules by holding it in an assembly with a curvature very similar to that of the depolymerization products of microtubules.

PubMed: 11030624
DOI: 10.1016/S0092-8674(00)00069-6

Experimental method

X-RAY DIFFRACTION (3.95 Å)