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  Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA

Taschner, M., Vetter, M., & Lorentzen, E. (2012). Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 109(48), 19649-19654. doi:10.1073/pnas.1209343109.

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 Creators:
Taschner, Michael1, Author           
Vetter, Melanie1, Author           
Lorentzen, Esben1, Author           
Affiliations:
1Lorentzen, Esben / Intraflagellar Transport, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565157              

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Free keywords: HISTONE DEACETYLASE INHIBITORS; MICROTUBULES; SUPERFAMILY; MECHANISMS; P300/CBP; DOMAIN; SITEcilium; crystal structure; post-translational modification;
 Abstract: Acetylation of lysine residues is an important posttranslational modification found in all domains of life. alpha-tubulin is specifically acetylated on lysine 40, a modification that serves to stabilize microtubules of axons and cilia. Whereas histone acetyltransferases have been extensively studied, there is no structural and mechanistic information available on alpha-tubulin acetyltransferases. Here, we present the structure of the human alpha-tubulin acetyltransferase catalytic domain bound to its cosubstrate acetyl-CoA at 1.05 angstrom resolution. Compared with other lysine acetyltransferases of known structure, alpha-tubulin acetyltransferase displays a relatively well-conserved cosubstrate binding pocket but is unique in its active site and putative alpha-tubulin binding site. Using acetylation assays with structure-guided mutants, we map residues important for acetylCoA binding, substrate binding, and catalysis. This analysis reveals a basic patch implicated in substrate binding and a conserved glutamine residue required for catalysis, demonstrating that the family of alpha-tubulin acetyltransferases uses a reaction mechanism different from other lysine acetyltransferases characterized to date.

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Language(s): eng - English
 Dates: 2012-11-27
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000312313900036
DOI: 10.1073/pnas.1209343109
 Degree: -

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Title: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Source Genre: Journal
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Publ. Info: 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA : NATL ACAD SCIENCES
Pages: - Volume / Issue: 109 (48) Sequence Number: - Start / End Page: 19649 - 19654 Identifier: ISSN: 0027-8424