4b5p

Crystal structure of human alpha tubulin acetyltransferase catalytic domain Q58A variant

spinqualitylabelsall models 4b5p, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4b5p is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACO, NA Related: 4b5o Activity: Alpha-tubulin N-acetyltransferase, with EC number 2.3.1.108 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ATAT_HUMAN] Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. May affect microtubule stability and regulate microtubule dynamics. May be involved in neuron development. Publication Abstract from PubMed 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 A 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 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 alpha-tubulin acetyltransferases uses a reaction mechanism different from other lysine acetyltransferases characterized to date. Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA.,Taschner M, Vetter M, Lorentzen E Proc Natl Acad Sci U S A. 2012 Nov 27;109(48):19649-54. doi:, 10.1073/pnas.1209343109. Epub 2012 Oct 15. PMID:23071318 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alpha-tubulin N-acetyltransferase 3D structures Tubulin acetyltransferase

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