9GNG
mouse VDAC1 in complex with MPD
Summary for 9GNG
| Entry DOI | 10.2210/pdb9gng/pdb |
| Descriptor | Isoform Mt-VDAC1 of Non-selective voltage-gated ion channel VDAC1, (4S)-2-METHYL-2,4-PENTANEDIOL, 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, ... (4 entities in total) |
| Functional Keywords | ion channel, va binding site, nadh, membrane protein |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 32993.06 |
| Authors | Lolicato, M.,Arrigoni, C. (deposition date: 2024-09-03, release date: 2025-01-08, Last modification date: 2025-01-22) |
| Primary citation | Conti Nibali, S.,Magri, A.,Messina, A.,Wagner, A.,Duman, R.,De Pinto, V.,Turato, C.,Arrigoni, C.,Lolicato, M. Protocol for high-yield bacterial expression and purification of the voltage-dependent anion channel 1 for high-throughput biophysical assays. STAR Protoc, 6:103557-103557, 2025 Cited by PubMed Abstract: Voltage-dependent anion channel 1 (VDAC1) is a key protein in cellular metabolism and apoptosis. Here, we present a protocol to express and purify milligram amounts of recombinant VDAC1 in Escherichia coli. We detail steps for a fluorescence polarization-based high-throughput screening assay using NADH displacement, along with procedures for thermostability, fluorescence polarization, and X-ray crystallography. In this context, we demonstrate how 2-methyl-2,4-pentanediol (MPD), a crystallization reagent, interferes with VDAC1 small-molecule binding, hindering the detection of these ligands in the crystal. For complete details on the use and execution of this protocol, please refer to Conti Nibali et al.. PubMed: 39799574DOI: 10.1016/j.xpro.2024.103557 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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