4F5U
Crystal structure of Equine Serum Albumin at 2.04 resolution
Summary for 4F5U
| Entry DOI | 10.2210/pdb4f5u/pdb |
| Related | 4F5S 4F5T 4F5V |
| Descriptor | Serum albumin, MALONATE ION, SUCCINIC ACID, ... (5 entities in total) |
| Functional Keywords | equine serum albumin, helical protein, transport protein |
| Biological source | Equus caballus (domestic horse,equine) |
| Cellular location | Secreted: P35747 |
| Total number of polymer chains | 1 |
| Total formula weight | 66718.65 |
| Authors | Bujacz, A.,Bujacz, G. (deposition date: 2012-05-13, release date: 2012-10-03, Last modification date: 2024-10-30) |
| Primary citation | Bujacz, A. Structures of bovine, equine and leporine serum albumin. Acta Crystallogr.,Sect.D, 68:1278-1289, 2012 Cited by PubMed Abstract: Serum albumin first appeared in early vertebrates and is present in the plasma of all mammals. Its canonical structure supported by a conserved set of disulfide bridges is maintained in all mammalian serum albumins and any changes in sequence are highly correlated with evolution of the species. Previous structural investigations of mammalian serum albumins have only concentrated on human serum albumin (HSA), most likely as a consequence of crystallization and diffraction difficulties. Here, the crystal structures of serum albumins isolated from bovine, equine and leporine blood plasma are reported. The structure of bovine serum albumin (BSA) was determined at 2.47 Å resolution, two crystal structures of equine serum albumin (ESA) were determined at resolutions of 2.32 and 2.04 Å, and that of leporine serum albumin (LSA) was determined at 2.27 Å resolution. These structures were compared in detail with the structure of HSA. The ligand-binding pockets in BSA, ESA and LSA revealed different amino-acid compositions and conformations in comparison to HSA in some cases; however, much more significant differences were observed on the surface of the molecules. BSA, which is one of the most extensively utilized proteins in laboratory practice and is used as an HSA substitute in many experiments, exhibits only 75.8% identity compared with HSA. The higher resolution crystal structure of ESA highlights the binding properties of this protein because it includes several bound compounds from the crystallization solution that provide additional structural information about potential ligand-binding pockets. PubMed: 22993082DOI: 10.1107/S0907444912027047 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.04 Å) |
Structure validation
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