1hku: Difference between revisions
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==Overview== | ==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 . | 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== | ==About this Structure== | ||
1HKU is a | 1HKU 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, GOL and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HKU OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transcription co-repression]] | [[Category: transcription co-repression]] | ||
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Revision as of 10:41, 5 November 2007
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CTBP/BARS: A DUAL-FUNCTION PROTEIN INVOLVED IN TRANSCRIPTION COREPRESSION AND GOLGI MEMBRANE FISSION
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
1HKU is a Single protein structure of sequence from Rattus norvegicus with NAD, GOL and FMT as ligands. 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
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