1hku
From Proteopedia
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==Overview== | ==Overview== | ||
| - | C-terminal-binding protein/brefeldin A-ADP ribosylated substrate | + | 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== | ||
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[[Category: transcription co-repression]] | [[Category: transcription co-repression]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:17 2008'' |
Revision as of 11:02, 21 February 2008
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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 , and as ligands. Known structural/functional Site: . 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 Thu Feb 21 13:02:17 2008
Categories: Rattus norvegicus | Single protein | Bolognesi, M. | Cericola, C. | Corda, D. | Luini, A. | Massaro, A. | Millo, E. | Nardini, M. | Pesce, A. | Spano , S. | FMT | GOL | NAD | Acyl-coa | Acyltransferase | Brefeldin a | Golgi membrane | Nad | Transcription co-repression
