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==Crystal structure of polyamine oxidase FMS1 from Saccharomyces cerevisiae in complex with bis-(3R,3'R)-methylated spermine==
==Crystal structure of polyamine oxidase FMS1 from Saccharomyces cerevisiae in complex with bis-(3R,3'R)-methylated spermine==
<StructureSection load='3bnm' size='340' side='right' caption='[[3bnm]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3bnm' size='340' side='right'caption='[[3bnm]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3bnm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BNM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BNM FirstGlance]. <br>
<table><tr><td colspan='2'>[[3bnm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BNM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BNM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SPJ:(3R,3R)-N~1~,N~1~-BUTANE-1,4-DIYLDIBUTANE-1,3-DIAMINE'>SPJ</scene></td></tr>
</td></tr><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=SPJ:(3R,3R)-N~1~,N~1~-BUTANE-1,4-DIYLDIBUTANE-1,3-DIAMINE'>SPJ</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bnu|3bnu]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bnu|3bnu]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FMS1, YMR020W, YM9711.09 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FMS1, YMR020W, YM9711.09 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17 1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17 1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bnm OCA], [http://pdbe.org/3bnm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bnm RCSB], [http://www.ebi.ac.uk/pdbsum/3bnm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bnm ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bnm OCA], [https://pdbe.org/3bnm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bnm RCSB], [https://www.ebi.ac.uk/pdbsum/3bnm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bnm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>   
[[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Hao, Q]]
[[Category: Hao, Q]]

Revision as of 11:19, 19 January 2022

Crystal structure of polyamine oxidase FMS1 from Saccharomyces cerevisiae in complex with bis-(3R,3'R)-methylated spermineCrystal structure of polyamine oxidase FMS1 from Saccharomyces cerevisiae in complex with bis-(3R,3'R)-methylated spermine

Structural highlights

3bnm is a 2 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:FMS1, YMR020W, YM9711.09 (ATCC 18824)
Activity:Oxidoreductase, with EC number 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17 1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17
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.

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

3bnm, resolution 2.20Å

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