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The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor.


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.

SUBMITTER: Korolev S 

PROVIDER: S-EPMC2792006 | biostudies-literature | 2002 Jan

REPOSITORIES: biostudies-literature

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The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor.

Korolev Sergey S   Ikeguchi Yoshihiko Y   Skarina Tatiana T   Beasley Steven S   Arrowsmith Cheryl C   Edwards Aled A   Joachimiak Andrzej A   Pegg Anthony E AE   Savchenko Alexei A  

Nature structural biology 20020101 1


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  ...[more]

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