4V2L
Crystallographic structure of thioredoxin from Litopenaeus vannamei: Radiation damage effect at 3.4 MGy, focused in disulfide bonds.
Summary for 4V2L
| Entry DOI | 10.2210/pdb4v2l/pdb |
| Related | 4V2M 4V2N |
| Descriptor | THIOREDOXIN, GLYCEROL, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | oxidoreductase, thioredoxin, shrimp, litopenaeus vannamie, radiation damage, disulfide bond |
| Biological source | LITOPENAEUS VANNAMEI (PACIFIC WHITE SHRIMP) |
| Total number of polymer chains | 2 |
| Total formula weight | 24256.71 |
| Authors | Campos-Acevedo, A.A.,Rudino-Pinera, E. (deposition date: 2014-10-10, release date: 2015-01-14, Last modification date: 2024-10-16) |
| Primary citation | Campos-Acevedo, A.A.,Rudino-Pinera, E. Crystallographic Studies Evidencing the High Energy Tolerance to Disrupting the Interface Disulfide Bond of Thioredoxin 1 from White Leg Shrimp Litopenaeus Vannamei. Molecules, 19:21113-, 2014 Cited by PubMed Abstract: Thioredoxin (Trx) is a small 12-kDa redox protein that catalyzes the reduction of disulfide bonds in proteins from different biological systems. A recent study of the crystal structure of white leg shrimp thioredoxin 1 from Litopenaeus vannamei (LvTrx) revealed a dimeric form of the protein mediated by a covalent link through a disulfide bond between Cys73 from each monomer. In the present study, X-ray-induced damage in the catalytic and the interface disulfide bond of LvTrx was studied at atomic resolution at different transmission energies of 8% and 27%, 12.8 keV at 100 K in the beamline I-24 at Diamond Light Source. We found that at an absorbed dose of 32 MGy, the X-ray induces the cleavage of the disulfide bond of each catalytic site; however, the interface disulfide bond was cleaved at an X-ray adsorbed dose of 85 MGy; despite being the most solvent-exposed disulfide bond in LvTrx (~50 Å2). This result clearly established that the interface disulfide bond is very stable and, therefore, less susceptible to being reduced by X-rays. In fact, these studies open the possibility of the existence in solution of a dimeric LvTrx. PubMed: 25517346DOI: 10.3390/MOLECULES191221113 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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