1hl3: Difference between revisions

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.

1HL3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with NAD as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HL3 OCA].  

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