1yy5

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[[Image:1yy5.gif|left|200px]]<br /><applet load="1yy5" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yy5.gif|left|200px]]
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caption="1yy5, resolution 2.30&Aring;" />
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'''Crystal structure of Fms1, a polyamine oxidase from Yeast'''<br />
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{{Structure
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|PDB= 1yy5 |SIZE=350|CAPTION= <scene name='initialview01'>1yy5</scene>, resolution 2.30&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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|ACTIVITY= [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]
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|GENE= FMS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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}}
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'''Crystal structure of Fms1, a polyamine oxidase from Yeast'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1YY5 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=1YY5 OCA].
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1YY5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YY5 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15843025 15843025]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15843025 15843025]
[[Category: Polyamine oxidase]]
[[Category: Polyamine oxidase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: polyamine oxidase]]
[[Category: polyamine oxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:28:55 2008''

Revision as of 13:28, 20 March 2008


PDB ID 1yy5

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands:
Gene: FMS1 (Saccharomyces cerevisiae)
Activity: Polyamine oxidase, with EC number 1.5.3.11
Coordinates: save as pdb, mmCIF, xml



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

1YY5 is a Single protein structure of sequence from Saccharomyces cerevisiae. 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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