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[[Image:1xpq.gif|left|200px]]


{{Structure
==Crystal structure of fms1, a polyamine oxidase from yeast==
|PDB= 1xpq |SIZE=350|CAPTION= <scene name='initialview01'>1xpq</scene>, resolution 2.60&Aring;
<StructureSection load='1xpq' size='340' side='right'caption='[[1xpq]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SPM:SPERMINE'>SPM</scene>
<table><tr><td colspan='2'>[[1xpq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XPQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XPQ FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.51&#8491;</td></tr>
|GENE= FMS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SPM:SPERMINE'>SPM</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xpq OCA], [https://pdbe.org/1xpq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xpq RCSB], [https://www.ebi.ac.uk/pdbsum/1xpq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xpq ProSAT]</span></td></tr>
|RELATEDENTRY=[[1rsg|1rsg]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xpq OCA], [http://www.ebi.ac.uk/pdbsum/1xpq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xpq RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/FMS1_YEAST FMS1_YEAST] Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.<ref>PMID:12670477</ref> <ref>PMID:14617780</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xp/1xpq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xpq ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''Crystal structure of fms1, a polyamine oxidase from yeast'''
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<ref>PMID:15843025</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1xpq" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Polyamine oxidase|Polyamine oxidase]]
 
== References ==
==About this Structure==
<references/>
1XPQ 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=1XPQ OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Hao Q]]
[[Category: Hao, Q.]]
[[Category: Huang Q]]
[[Category: Huang, Q.]]
[[Category: Liu Q]]
[[Category: Liu, Q.]]
[[Category: complex]]
[[Category: crystal structure]]
[[Category: polyamine oxidase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:52:57 2008''

Latest revision as of 10:56, 15 May 2024

Crystal structure of fms1, a polyamine oxidase from yeastCrystal structure of fms1, a polyamine oxidase from yeast

Structural highlights

1xpq is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.51Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FMS1_YEAST Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Landry J, Sternglanz R. Yeast Fms1 is a FAD-utilizing polyamine oxidase. Biochem Biophys Res Commun. 2003 Apr 11;303(3):771-6. PMID:12670477
  2. ↑ Chattopadhyay MK, Tabor CW, Tabor H. Spermidine but not spermine is essential for hypusine biosynthesis and growth in Saccharomyces cerevisiae: spermine is converted to spermidine in vivo by the FMS1-amine oxidase. Proc Natl Acad Sci U S A. 2003 Nov 25;100(24):13869-74. Epub 2003 Nov 14. PMID:14617780 doi:http://dx.doi.org/10.1073/pnas.1835918100
  3. ↑ Huang Q, Liu Q, Hao Q. Crystal structures of Fms1 and its complex with spermine reveal substrate specificity. J Mol Biol. 2005 May 13;348(4):951-9. PMID:15843025 doi:10.1016/j.jmb.2005.03.008

1xpq, resolution 2.51Å

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