1ryi

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[[Image:1ryi.gif|left|200px]]
[[Image:1ryi.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1ryi |SIZE=350|CAPTION= <scene name='initialview01'>1ryi</scene>, resolution 1.80&Aring;
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The line below this paragraph, containing "STRUCTURE_1ryi", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOA:GLYCOLIC+ACID'>GOA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= GOXB, BSU11670 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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-->
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|DOMAIN=
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{{STRUCTURE_1ryi| PDB=1ryi | SCENE= }}
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|RELATEDENTRY=[[1ng3|1NG3]], [[1ng4|1NG4]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ryi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ryi OCA], [http://www.ebi.ac.uk/pdbsum/1ryi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ryi RCSB]</span>
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}}
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'''STRUCTURE OF GLYCINE OXIDASE WITH BOUND INHIBITOR GLYCOLATE'''
'''STRUCTURE OF GLYCINE OXIDASE WITH BOUND INHIBITOR GLYCOLATE'''
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[[Category: Pollegioni, L.]]
[[Category: Pollegioni, L.]]
[[Category: Welte, W.]]
[[Category: Welte, W.]]
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[[Category: flavoprotein]]
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[[Category: Flavoprotein]]
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[[Category: oxidase]]
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[[Category: Oxidase]]
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[[Category: protein-inhibitor complex]]
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[[Category: Protein-inhibitor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:03:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:34:51 2008''
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Revision as of 05:03, 3 May 2008

Template:STRUCTURE 1ryi

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. 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 Page seeded by OCA on Sat May 3 08:03:58 2008

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