2E5V
Crystal structure of L-Aspartate Oxidase from hyperthermophilic archaeon Sulfolobus tokodaii
Summary for 2E5V
| Entry DOI | 10.2210/pdb2e5v/pdb |
| Descriptor | L-aspartate oxidase, CHLORIDE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | l-aspartate oxidase, archaea, oxidoreductase |
| Biological source | Sulfolobus tokodaii |
| Cellular location | Cytoplasm (By similarity): Q972D2 |
| Total number of polymer chains | 2 |
| Total formula weight | 106949.28 |
| Authors | Yoneda, K.,Sakuraba, H.,Asai, I.,Tsuge, H.,Katunuma, N.,Ohshima, T. (deposition date: 2006-12-25, release date: 2008-01-01, Last modification date: 2024-03-13) |
| Primary citation | Sakuraba, H.,Yoneda, K.,Asai, I.,Tsuge, H.,Katunuma, N.,Ohshima, T. Structure of l-aspartate oxidase from the hyperthermophilic archaeon Sulfolobus tokodaii Biochim.Biophys.Acta, 1784:563-571, 2008 Cited by PubMed Abstract: The crystal structure of the highly thermostable l-aspartate oxidase (LAO) from the hyperthermophilic archaeon Sulfolobus tokodaii was determined at a 2.09 A resolution. The factors contributing to the thermostability of the enzyme were analyzed by comparing its structure to that of Escherichia coli LAO. Like E. coli LAO, the S. tokodaii enzyme consists of three domains: an FAD-binding domain, an alpha+beta capping domain, and a C-terminal three-helix bundle. However, the situation of the linker between the FAD-binding domain and C-terminal three-helix bundle in S. tokodaii LAO is completely different from that in E. coli LAO, where the linker is situated near the FAD-binding domain and has virtually no interaction with the rest of the protein. In S. tokodaii LAO, this linker is situated near the C-terminal three-helix bundle and contains a beta-strand that runs parallel to the C-terminal strand. This results in the formation of an additional beta-sheet, which appears to reduce the flexibility of the C-terminal region. Furthermore, the displacement of the linker enables formation of a 5-residue ion-pair network between the FAD-binding and C-terminal domains, which strengthens the interdomain interactions. These features might be the main factors contributing to the high thermostability of S. tokodaii LAO. PubMed: 18226609DOI: 10.1016/j.bbapap.2007.12.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.09 Å) |
Structure validation
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