1rsg
From Proteopedia
(New page: 200px<br /><applet load="1rsg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rsg, resolution 1.90Å" /> '''Crystal structure of...) |
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| - | [[Image:1rsg.gif|left|200px]]<br /><applet load="1rsg" size=" | + | [[Image:1rsg.gif|left|200px]]<br /><applet load="1rsg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rsg, resolution 1.90Å" /> | caption="1rsg, resolution 1.90Å" /> | ||
'''Crystal structure of the polyamine oxidase Fms1 from yeast'''<br /> | '''Crystal structure of the polyamine oxidase Fms1 from yeast'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Fms1 is a rate-limiting enzyme for the biosynthesis of pantothenic acid in | + | 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== | ==About this Structure== | ||
| - | 1RSG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Polyamine_oxidase Polyamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.11 1.5.3.11] Full crystallographic information is available from [http:// | + | 1RSG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Polyamine_oxidase Polyamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.11 1.5.3.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: fad binding motif]] | [[Category: fad binding motif]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:54:07 2008'' |
Revision as of 12:54, 21 February 2008
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Crystal structure of the polyamine oxidase Fms1 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
1RSG is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Active as Polyamine oxidase, with EC number 1.5.3.11 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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