1JQ3
Crystal Structure of Spermidine Synthase in Complex with Transition State Analogue AdoDATO
Summary for 1JQ3
| Entry DOI | 10.2210/pdb1jq3/pdb |
| Related | 1INL |
| Descriptor | Spermidine synthase, S-ADENOSYL-1,8-DIAMINO-3-THIOOCTANE (3 entities in total) |
| Functional Keywords | aminopropyltransferase, homo-tetramer, thermophyle, transition-state analogue, beta-barrel, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, transferase |
| Biological source | Thermotoga maritima |
| Total number of polymer chains | 4 |
| Total formula weight | 138006.75 |
| Authors | Korolev, S.,Ikeguchi, Y.,Skarina, T.,Beasley, S.,Edwards, A.,Joachimiak, A.,Pegg, A.E.,Savchenko, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2001-08-03, release date: 2001-11-21, Last modification date: 2023-08-16) |
| Primary citation | Korolev, S.,Ikeguchi, Y.,Skarina, T.,Beasley, S.,Arrowsmith, C.,Edwards, A.,Joachimiak, A.,Pegg, A.E.,Savchenko, A. The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor. Nat.Struct.Biol., 9:27-31, 2002 Cited by PubMed Abstract: Polyamines are essential in all branches of life. Spermidine synthase (putrescine aminopropyltransferase, PAPT) catalyzes the biosynthesis of spermidine, a ubiquitous polyamine. The crystal structure of the PAPT from Thermotoga maritima (TmPAPT) has been solved to 1.5 A resolution in the presence and absence of AdoDATO (S-adenosyl-1,8-diamino-3-thiooctane), a compound containing both substrate and product moieties. This, the first structure of an aminopropyltransferase, reveals deep cavities for binding substrate and cofactor, and a loop that envelops the active site. The AdoDATO binding site is lined with residues conserved in PAPT enzymes from bacteria to humans, suggesting a universal catalytic mechanism. Other conserved residues act sterically to provide a structural basis for polyamine specificity. The enzyme is tetrameric; each monomer consists of a C-terminal domain with a Rossmann-like fold and an N-terminal beta-stranded domain. The tetramer is assembled using a novel barrel-type oligomerization motif. PubMed: 11731804DOI: 10.1038/nsb737 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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