7QNO

Crystal structure of ligand-free Danio rerio HDAC6 CD1 CD2

Summary for 7QNO

• Entry DOI: 10.2210/pdb7qno/pdb
• Descriptor: Histone deacetylase 6, PROLINE, POTASSIUM ION, ... (6 entities in total)
• Functional Keywords: deacetylase, histone, microtuble, transport protein
• Biological source: Danio rerio (zebrafish)
• Total number of polymer chains: 1
• Total formula weight: 92840.66

Authors

Kempf, G.,Langousis, G.,Sanchez, J.,Matthias, P. (deposition date: 2021-12-21, release date: 2022-02-09, Last modification date: 2024-01-31)

Primary citation

Langousis, G.,Sanchez, J.,Kempf, G.,Matthias, P.
Expression and Crystallization of HDAC6 Tandem Catalytic Domains.
Methods Mol.Biol., 2589:467-480, 2023

PubMed Abstract: Histone deacetylase 6 (HDAC6) is an atypical lysine deacetylase with tandem catalytic domains and an ubiquitin-binding zinc finger domain. HDAC6 is involved in various biological processes, such as cell motility or stress responses, and has been implicated in pathologies ranging from cancer to neurodegeneration. Due to this broad range of functions, there has been considerable interest in developing HDAC6-specific small molecule inhibitors, several of which are already available. The crystal structure of the tandem catalytic domains of zebrafish HDAC6 has revealed an arrangement with twofold symmetry and extensive surface interaction between the catalytic domains. Further dissection of the biochemical properties of HDAC6 and the development of novel inhibitors will benefit from being able to routinely express high-quality protein. We present here our optimized protocol for expression and crystallization of the zebrafish tandem catalytic domains.

PubMed: 36255643
DOI: 10.1007/978-1-0716-2788-4_30

Experimental method

X-RAY DIFFRACTION (2.38 Å)