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4B5P

Crystal structure of human alpha tubulin acetyltransferase catalytic domain Q58A variant

Summary for 4B5P
Entry DOI10.2210/pdb4b5p/pdb
Related4B5O
DescriptorALPHA-TUBULIN N-ACETYLTRANSFERASE, SODIUM ION, ACETYL COENZYME *A, ... (5 entities in total)
Functional Keywordstransferase, lysine acetyltransferase, acetyl coa, tubulin, microtubules, cilium, intraflagellar transport
Biological sourceHOMO SAPIENS (HUMAN)
More
Total number of polymer chains2
Total formula weight47249.38
Authors
Taschner, M.,Vetter, M.,Lorentzen, E. (deposition date: 2012-08-07, release date: 2012-10-24, Last modification date: 2023-12-20)
Primary citationTaschner, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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数据于2025-07-09公开中

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