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1HL3

CtBP/BARS in ternary complex with NAD(H) and PIDLSKK peptide

Summary for 1HL3
Entry DOI10.2210/pdb1hl3/pdb
DescriptorC-TERMINAL BINDING PROTEIN 3, PRO-ILE-ASP-LEU-SER-LYS-LYS PEPTIDE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
Functional Keywordstrancription co-repressor, transcription co-repression, acyltransferase, brefeldin a, nad, golgi membrane, acyl-coa
Biological sourceRATTUS NORVEGICUS (RAT)
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Cellular locationCytoplasm : Q9Z2F5
Total number of polymer chains2
Total formula weight40974.53
Authors
Nardini, M.,Spano, S.,Cericola, C.,Pesce, A.,Massaro, A.,Millo, E.,Luini, A.,Corda, D.,Bolognesi, M. (deposition date: 2003-03-13, release date: 2003-06-19, Last modification date: 2023-12-13)
Primary citationNardini, M.,Spano, S.,Cericola, C.,Pesce, A.,Massaro, A.,Millo, E.,Luini, A.,Corda, D.,Bolognesi, M.
Ctbp/Bars: A Dual-Function Protein Involved in Transcription Co-Repression and Golgi Membrane Fission
Embo J., 22:3122-, 2003
Cited by
PubMed Abstract: 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.
PubMed: 12805226
DOI: 10.1093/EMBOJ/CDG283
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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数据于2025-07-02公开中

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