1xpq
Crystal structure of fms1, a polyamine oxidase from yeast
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| , resolution 2.60Å | |||||||
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| Ligands: | and | ||||||
| Gene: | FMS1 (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
Fms1 is a rate-limiting enzyme for the biosynthesis of pantothenic acid in yeast. Fms1 has polyamine oxidase (PAO) activity, which converts spermine into spermidine and 3-aminopropanal. The 3-aminopropanal is further oxidized to produce beta-alanine, which is necessary for the biosynthesis of pantothenic acid. The crystal structures of Fms1 and its complex with the substrate spermine have been determined using the single-wavelength anomalous diffraction (SAD) phasing method. Fms1 consists of an FAD-binding domain, with Rossmann fold topology, and a substrate-binding domain. The active site is a tunnel located at the interface of the two domains. The substrate spermine binds to the active site mainly via hydrogen bonds and hydrophobic interactions. In the complex, C11 but not C9 of spermine is close enough to the catalytic site (N5 of FAD) to be oxidized. Therefore, the products are spermidine and 3-aminopropanal, rather than 3-(aminopropyl) 4-aminobutyraldehyde and 1,3-diaminoprone.
About this StructureAbout this Structure
1XPQ is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of Fms1 and its complex with spermine reveal substrate specificity., Huang Q, Liu Q, Hao Q, J Mol Biol. 2005 May 13;348(4):951-9. PMID:15843025
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