1ryi
From Proteopedia
(New page: 200px<br /><applet load="1ryi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ryi, resolution 1.80Å" /> '''STRUCTURE OF GLYCINE...) |
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| - | [[Image:1ryi.gif|left|200px]]<br /><applet load="1ryi" size=" | + | [[Image:1ryi.gif|left|200px]]<br /><applet load="1ryi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ryi, resolution 1.80Å" /> | caption="1ryi, resolution 1.80Å" /> | ||
'''STRUCTURE OF GLYCINE OXIDASE WITH BOUND INHIBITOR GLYCOLATE'''<br /> | '''STRUCTURE OF GLYCINE OXIDASE WITH BOUND INHIBITOR GLYCOLATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Structure-function relationships of the flavoprotein glycine oxidase (GO), which was recently proposed as the first enzyme in the biosynthesis of | + | Structure-function relationships of the flavoprotein glycine oxidase (GO), which was recently proposed as the first enzyme in the biosynthesis of thiamine in Bacillus subtilis, has been investigated by a combination of structural and functional studies. The structure of the GO-glycolate complex was determined at 1.8 A, a resolution at which a sketch of the residues involved in FAD binding and in substrate interaction can be depicted. GO can be considered a member of the "amine oxidase" class of flavoproteins, such as d-amino acid oxidase and monomeric sarcosine oxidase. With the obtained model of GO the monomer-monomer interactions can be analyzed in detail, thus explaining the structural basis of the stable tetrameric oligomerization state of GO, which is unique for the GR(2) subfamily of flavooxidases. On the other hand, the three-dimensional structure of GO and the functional experiments do not provide the functional significance of such an oligomerization state; GO does not show an allosteric behavior. The results do not clarify the metabolic role of this enzyme in B. subtilis; the broad substrate specificity of GO cannot be correlated with the inferred function in thiamine biosynthesis, and the structure does not show how GO could interact with ThiS, the following enzyme in thiamine biosynthesis. However, they do let a general catabolic role of this enzyme on primary or secondary amines to be excluded because the expression of GO is not inducible by glycine, sarcosine, or d-alanine as carbon or nitrogen sources. |
==About this Structure== | ==About this Structure== | ||
| - | 1RYI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with FAD and GOA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glycine_oxidase Glycine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.19 1.4.3.19] Full crystallographic information is available from [http:// | + | 1RYI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=GOA:'>GOA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glycine_oxidase Glycine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.19 1.4.3.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RYI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Molla, G.]] | [[Category: Molla, G.]] | ||
[[Category: Motteran, L.]] | [[Category: Motteran, L.]] | ||
| - | [[Category: Pilone, M | + | [[Category: Pilone, M S.]] |
[[Category: Pollegioni, L.]] | [[Category: Pollegioni, L.]] | ||
[[Category: Welte, W.]] | [[Category: Welte, W.]] | ||
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[[Category: flavoprotein; oxidase; protein-inhibitor complex]] | [[Category: flavoprotein; oxidase; protein-inhibitor complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:55 2008'' |
Revision as of 12:55, 21 February 2008
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STRUCTURE OF GLYCINE OXIDASE WITH BOUND INHIBITOR GLYCOLATE
Overview
Structure-function relationships of the flavoprotein glycine oxidase (GO), which was recently proposed as the first enzyme in the biosynthesis of thiamine in Bacillus subtilis, has been investigated by a combination of structural and functional studies. The structure of the GO-glycolate complex was determined at 1.8 A, a resolution at which a sketch of the residues involved in FAD binding and in substrate interaction can be depicted. GO can be considered a member of the "amine oxidase" class of flavoproteins, such as d-amino acid oxidase and monomeric sarcosine oxidase. With the obtained model of GO the monomer-monomer interactions can be analyzed in detail, thus explaining the structural basis of the stable tetrameric oligomerization state of GO, which is unique for the GR(2) subfamily of flavooxidases. On the other hand, the three-dimensional structure of GO and the functional experiments do not provide the functional significance of such an oligomerization state; GO does not show an allosteric behavior. The results do not clarify the metabolic role of this enzyme in B. subtilis; the broad substrate specificity of GO cannot be correlated with the inferred function in thiamine biosynthesis, and the structure does not show how GO could interact with ThiS, the following enzyme in thiamine biosynthesis. However, they do let a general catabolic role of this enzyme on primary or secondary amines to be excluded because the expression of GO is not inducible by glycine, sarcosine, or d-alanine as carbon or nitrogen sources.
About this Structure
1RYI is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Active as Glycine oxidase, with EC number 1.4.3.19 Full crystallographic information is available from OCA.
Reference
Structure-function correlation in glycine oxidase from Bacillus subtilis., Mortl M, Diederichs K, Welte W, Molla G, Motteran L, Andriolo G, Pilone MS, Pollegioni L, J Biol Chem. 2004 Jul 9;279(28):29718-27. Epub 2004 Apr 22. PMID:15105420
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