1rsg

From Proteopedia

(Difference between revisions)

Revision as of 15:17, 11 September 2015

Crystal structure of the polyamine oxidase Fms1 from yeast

Structural highlights

1rsg 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:
NonStd Res:
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

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.

References

↑ 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
↑ 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
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 2: / Line 2: @@
 <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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RSG FirstGlance]. <br>
+<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RSG 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></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 Saccharomyces cerevisiae])</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rsg RCSB], [http://www.ebi.ac.uk/pdbsum/1rsg PDBsum]</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=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]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1rsg" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 37: @@
 __TOC__
 </StructureSection>
+[[Category: Atcc 18824]]
 [[Category: Oxidoreductase]]
-[[Category: Saccharomyces cerevisiae]]
 [[Category: Hao, Q]]
 [[Category: Huang, Q]]
 [[Category: Liu, Q]]
 [[Category: Fad binding motif]]

1rsg

From Proteopedia

Revision as of 15:17, 11 September 2015

Crystal structure of the polyamine oxidase Fms1 from yeast

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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