1xpq
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(New page: 200px<br /><applet load="1xpq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xpq, resolution 2.60Å" /> '''Crystal structure of...)
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Revision as of 04:07, 21 November 2007
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Crystal structure of fms1, a polyamine oxidase from yeast
Overview
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 Structure
1XPQ is a Single protein structure of sequence from Saccharomyces cerevisiae with SPM and FAD as ligands. Full crystallographic information is available from OCA.
Reference
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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