1hl3
CtBP/BARS in ternary complex with NAD(H) and PIDLSKK peptide
Structural highlights
FunctionCTBP1_RAT Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Corepressor targeting diverse transcription regulators such as GLIS2. Has dehydrogenase activity. Functions in brown adipose tissue (BAT) differentiation.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedC-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. CtBP/BARS: a dual-function protein involved in transcription co-repression and Golgi membrane fission.,Nardini M, Spano S, Cericola C, Pesce A, Massaro A, Millo E, Luini A, Corda D, Bolognesi M EMBO J. 2003 Jun 16;22(12):3122-30. PMID:12805226[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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