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1rsg

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Crystal structure of the polyamine oxidase Fms1 from yeast

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rsg"

Categories: Large Structures | Saccharomyces cerevisiae | Hao Q | Huang Q | Liu Q

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-[[Image:1rsg.gif|left|200px]]<br /><applet load="1rsg" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1rsg, resolution 1.90&Aring;" />
-'''Crystal structure of the polyamine oxidase Fms1 from yeast'''<br />
-==Overview==
+==Crystal structure of the polyamine oxidase Fms1 from yeast==
-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.
+<StructureSection load='1rsg' size='340' side='right'caption='[[1rsg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1rsg]] is a 2 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=1RSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RSG FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=MSE:SELENOMETHIONINE'>MSE</scene></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=1rsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsg OCA], [https://pdbe.org/1rsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rsg RCSB], [https://www.ebi.ac.uk/pdbsum/1rsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rsg ProSAT]</span></td></tr>
+</table>
+== 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/rs/1rsg_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=1rsg ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-RSG 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RSG OCA].
+*[[Polyamine oxidase|Polyamine oxidase]]
+== References ==
-==Reference==
+<references/>
-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]
+__TOC__
-[[Category: Polyamine oxidase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[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: FAD]]
-[[Category: fad binding motif]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:50:25 2007''

1rsg

From Proteopedia

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Crystal structure of the polyamine oxidase Fms1 from yeast

Structural highlights

Function

Evolutionary Conservation

See Also

References

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