4B5O

Crystal structure of human alpha tubulin acetyltransferase catalytic domain

4B5O の概要

• エントリーDOI: 10.2210/pdb4b5o/pdb
• 関連するPDBエントリー: 4B5P
• 分子名称: ALPHA-TUBULIN N-ACETYLTRANSFERASE, SODIUM ION, ACETYL COENZYME *A, ... (4 entities in total)
• 機能のキーワード: transferase, microtubules, cilium, intraflagellar transport
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23674.73

構造登録者

Taschner, M.,Vetter, M.,Lorentzen, E. (登録日: 2012-08-07, 公開日: 2012-10-24, 最終更新日: 2024-05-08)

主引用文献

Taschner, M.,Vetter, M.,Lorentzen, E.
Atomic Resolution Structure of Human Alpha-Tubulin Acetyltransferase Bound to Acetyl-Coa.
Proc.Natl.Acad.Sci.USA, 109:19649-, 2012

PubMed Abstract: Acetylation of lysine residues is an important posttranslational modification found in all domains of life. α-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 α-tubulin acetyltransferases. Here, we present the structure of the human α-tubulin acetyltransferase catalytic domain bound to its cosubstrate acetyl-CoA at 1.05 Å resolution. Compared with other lysine acetyltransferases of known structure, α-tubulin acetyltransferase displays a relatively well-conserved cosubstrate binding pocket but is unique in its active site and putative α-tubulin binding site. Using acetylation assays with structure-guided mutants, we map residues important for acetyl-CoA 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 α-tubulin acetyltransferases uses a reaction mechanism different from other lysine acetyltransferases characterized to date.

PubMed: 23071318
DOI: 10.1073/PNAS.1209343109

実験手法

X-RAY DIFFRACTION (1.05 Å)