1YY5

Crystal structure of Fms1, a polyamine oxidase from Yeast

Summary for 1YY5

• Entry DOI: 10.2210/pdb1yy5/pdb
• Related: 1rsg 1xpq
• Descriptor: FMS1 protein, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: polyamine oxidase, fms1, oxidoreductase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 118629.40

Authors

Huang, Q.,Liu, Q.,Hao, Q. (deposition date: 2005-02-23, release date: 2005-03-08, Last modification date: 2024-10-30)

Primary citation

Huang, Q.,Liu, Q.,Hao, Q.
Crystal Structures of Fms1 and its Complex with Spermine Reveal Substrate Specificity.
J.Mol.Biol., 348:951-959, 2005

PubMed Abstract: 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.

PubMed: 15843025
DOI: 10.1016/j.jmb.2005.03.008

Experimental method

X-RAY DIFFRACTION (2.3 Å)