8IYI
Spermidine synthase from Kluyveromyces lactis
Summary for 8IYI
| Entry DOI | 10.2210/pdb8iyi/pdb |
| Descriptor | KLLA0B09372p (2 entities in total) |
| Functional Keywords | spermidine, synthase, aminopropyltransferase, transferase |
| Biological source | Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast, Candida sphaerica) |
| Total number of polymer chains | 2 |
| Total formula weight | 66585.56 |
| Authors | Kim, S.,Chang, J.H. (deposition date: 2023-04-05, release date: 2023-06-28, Last modification date: 2024-05-29) |
| Primary citation | Kim, S.,Chang, J.H. Structural Analysis of Spermidine Synthase from Kluyveromyces lactis. Molecules, 28:-, 2023 Cited by PubMed Abstract: Spermidine is a polyamine molecule that performs various cellular functions, such as DNA and RNA stabilization, autophagy modulation, and eIF5A formation, and is generated from putrescine by aminopropyltransferase spermidine synthase (SpdS). During synthesis, the aminopropyl moiety is donated from decarboxylated S-adenosylmethionine to form putrescine, with 5'-deoxy-5'-methylthioadenosine being produced as a byproduct. Although the molecular mechanism of SpdS function has been well-established, its structure-based evolutionary relationships remain to be fully understood. Moreover, only a few structural studies have been conducted on SpdS from fungal species. Here, we determined the crystal structure of an apo-form of SpdS from (SpdS) at 1.9 Å resolution. Structural comparison with its homologs revealed a conformational change in the α6 helix linked to the gate-keeping loop, with approximately 40° outward rotation. This change caused the catalytic residue Asp170 to move outward, possibly due to the absence of a ligand in the active site. These findings improve our understanding of the structural diversity of SpdS and provide a missing link that expands our knowledge of the structural features of SpdS in fungal species. PubMed: 37110680DOI: 10.3390/molecules28083446 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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