3GA0

CtBP1/BARS Gly172->Glu mutant structure: impairing NAD(H) binding and dimerization

Summary for 3GA0

• Entry DOI: 10.2210/pdb3ga0/pdb
• Related: 1HKU 1HL3 2HU2
• Descriptor: C-terminal-binding protein 1, FORMIC ACID (3 entities in total)
• Functional Keywords: transcription co-repression, acyltransferase, brefeldin a, nad, golgi membrane, acyl-coa, adp-ribosylation, cytoplasm, nucleus, oxidoreductase, phosphoprotein, ubl conjugation
• Biological source: Rattus norvegicus (Rat)
• Cellular location: Cytoplasm: Q9Z2F5
• Total number of polymer chains: 1
• Total formula weight: 39673.25

Authors

Nardini, M.,Valente, C.,Ricagno, S.,Luini, A.,Corda, D.,Bolognesi, M. (deposition date: 2009-02-16, release date: 2009-04-21, Last modification date: 2023-11-01)

Primary citation

Nardini, M.,Valente, C.,Ricagno, S.,Luini, A.,Corda, D.,Bolognesi, M.
CtBP1/BARS Gly172-->Glu mutant structure: impairing NAD(H)-binding and dimerization
Biochem.Biophys.Res.Commun., 381:70-74, 2009

PubMed Abstract: C-terminal binding proteins (CtBPs) are multi-functional proteins involved in nuclear transcriptional co-repression, Golgi membrane fission, and synaptic ribbon formation. Binding of NAD(H) to CtBPs promotes dimerization. CtBP dimers act as a scaffold for multimeric protein complex formation, thus bridging transcriptional repressors and their targets in the nucleus. Based on size-exclusion chromatography experiments and on the crystal structure of the NAD(H)-free G172E CtBP mutant, we show here that absence of NAD(H) induces flexibility/backbone conformational changes at the dimerization interface and at the CtBP interdomain region. The results presented shed first light on the correlation between NAD(H)-binding and functional CtBP dimerization.

PubMed: 19351597
DOI: 10.1016/j.bbrc.2009.02.010

Experimental method

X-RAY DIFFRACTION (3.4 Å)