1rsg

<table><tr><td colspan='2'>[[1rsg]] 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=1RSG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RSG FirstGlance]. <br>

</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></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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='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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1rsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsg OCA], [http://pdbe.org/1rsg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rsg RCSB], [http://www.ebi.ac.uk/pdbsum/1rsg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rsg ProSAT]</span></td></tr>

[[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>

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== 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<ref>PMID:15843025</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1rsg" style="background-color:#fffaf0;"></div>

[[Category: Atcc 18824]]

[[Category: Oxidoreductase]]

[[Category: Hao, Q]]

[[Category: Huang, Q]]

[[Category: Liu, Q]]

[[Category: Fad binding motif]]