1hl3
From Proteopedia
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CTBP/BARS IN TERNARY COMPLEX WITH NAD(H) AND PIDLSKK PEPTIDE
Overview
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.
About this Structure
1HL3 is a Single protein structure of sequence from Rattus norvegicus with NAD as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 5 15:31:42 2007
