1HKU

CtBP/BARS: a dual-function protein involved in transcription corepression and Golgi membrane fission

Summary for 1HKU

• Entry DOI: 10.2210/pdb1hku/pdb
• Descriptor: C-TERMINAL BINDING PROTEIN 3, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, GLYCEROL, ... (5 entities in total)
• Functional Keywords: transcription, transcription co-repressor, transcription co-repression, acyltransferase, brefeldin a, nad, golgi membrane, acyl-coa
• Biological source: RATTUS NORVEGICUS (NORWAY RAT)
• Cellular location: Cytoplasm : Q9Z2F5
• Total number of polymer chains: 1
• Total formula weight: 40372.70

Authors

Nardini, M.,Spano, S.,Cericola, C.,Pesce, A.,Massaro, A.,Millo, E.,Luini, A.,Corda, D.,Bolognesi, M. (deposition date: 2003-03-11, release date: 2003-06-19, Last modification date: 2024-11-20)

Primary citation

Nardini, M.,Spano, S.,Cericola, C.,Pesce, A.,Massaro, A.,Millo, E.,Luini, A.,Corda, D.,Bolognesi, M.
Ctbp/Bars: A Dual-Function Protein Involved in Transcription Co-Repression and Golgi Membrane Fission
Embo J., 22:3122-, 2003

PubMed Abstract: C-terminal-binding protein/brefeldin A-ADP ribosylated substrate (CtBP/BARS) plays key roles in development and oncogenesis as a transcription co-repressor, and in intracellular traffic as a promoter of Golgi membrane fission. Co-repressor activity is regulated by NAD(H) binding to CtBP/BARS, while membrane fission is associated with its acyl-CoA-dependent acyltransferase activity. Here, we report the crystal structures of rat CtBP/BARS in a binary complex with NAD(H), and in a ternary complex with a PIDLSKK peptide mimicking the consensus motif (PXDLS) recognized in CtBP/BARS cellular partners. The structural data show CtBP/BARS in a NAD(H)-bound dimeric form; the peptide binding maps the recognition site for DNA-binding proteins and histone deacetylases to an N-terminal region of the protein. The crystal structure together with the site-directed mutagenesis data and binding experiments suggest a rationale for the molecular mechanisms underlying the two fundamental co-existing, but diverse, activities supported by CtBP/BARS in the nucleus and in Golgi membranes.

PubMed: 12805226
DOI: 10.1093/EMBOJ/CDG283

Experimental method

X-RAY DIFFRACTION (2.3 Å)