3KXC
Mutant transport protein
Summary for 3KXC
| Entry DOI | 10.2210/pdb3kxc/pdb |
| Related | 2CFH |
| Descriptor | Trafficking protein particle complex subunit 3, Trafficking protein particle complex subunit 6B, PALMITIC ACID, ... (4 entities in total) |
| Functional Keywords | heterodimer, endoplasmic reticulum, er-golgi transport, golgi apparatus, lipoprotein, palmitate, transport, transport protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Golgi apparatus, cis-Golgi network (By similarity): O43617 Q86SZ2 |
| Total number of polymer chains | 2 |
| Total formula weight | 40146.13 |
| Authors | Kummel, D.,Heinemann, U. (deposition date: 2009-12-02, release date: 2010-04-21, Last modification date: 2023-11-01) |
| Primary citation | Kummel, D.,Walter, J.,Heck, M.,Heinemann, U.,Veit, M. Characterization of the self-palmitoylation activity of the transport protein particle component Bet3 Cell.Mol.Life Sci., 67:2653-2664, 2010 Cited by PubMed Abstract: Bet3, a transport protein particle component involved in vesicular trafficking, contains a hydrophobic tunnel occupied by a fatty acid linked to cysteine 68. We reported that Bet3 has a unique self-palmitoylating activity. Here we show that mutation of arginine 67 reduced self-palmitoylation of Bet3, but the effect was compensated by increasing the pH. Thus, arginine helps to deprotonate cysteine such that it could function as a nucleophile in the acylation reaction which is supported by the structural analysis of non-acylated Bet3. Using fluorescence spectroscopy we show that long-chain acyl-CoAs bind with micromolar affinity to Bet3, whereas shorter-chain acyl-CoAs do not interact. Mutants with a deleted acylation site or a blocked tunnel bind to Pal-CoA, only the latter with slightly reduced affinity. Bet3 contains three binding sites for Pal-CoA, but their number was reduced to two in the mutant with an obstructed tunnel, indicating that Bet3 contains binding sites on its surface. PubMed: 20372964DOI: 10.1007/s00018-010-0358-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
