Structure of the αβ tubulin dimer by electron crystallography View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1998-01

AUTHORS

Eva Nogales, Sharon G. Wolf, Kenneth H. Downing

ABSTRACT

The αβ tubulin heterodimer is the structural subunit of microtubules, which are cytoskeletal elements that are essential for intracellular transport and cell division in all eukaryotes. Each tubulin monomer binds a guanine nucleotide, which is non-exchangeable when it is bound in the α subunit, or N site, and exchangeable when bound in the β subunit, or E site. The α- and β-tubulins share 40% amino-acid sequence identity, both exist in several isotype forms, and both undergo a variety of post-translational modifications1. Limited sequence homology has been found with the proteins FtsZ2 and Misato3, which are involved in cell division in bacteria and Drosophila, respectively. Here we present an atomic model of the αβ tubulin dimer fitted to a 3.7-Å density map obtained by electron crystallography of zinc-induced tubulin sheets. The structures of α- and β-tubulin are basically identical: each monomer is formed by a core of two β-sheets surrounded by α-helices. The monomer structure is very compact, but can be divided into three functional domains: the amino-terminal domain containing the nucleotide-binding region, an intermediate domain containing the Taxol-binding site, and the carboxy-terminal domain, which probably constitutes the binding surface for motor proteins. More... »

PAGES

199-203

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/34465

DOI

http://dx.doi.org/10.1038/34465

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1016383987

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9428769


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