2ez4

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[[Image:2ez4.gif|left|200px]]<br /><applet load="2ez4" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ez4.gif|left|200px]]
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caption="2ez4, resolution 2.03&Aring;" />
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'''Pyruvate oxidase variant F479W'''<br />
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{{Structure
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|PDB= 2ez4 |SIZE=350|CAPTION= <scene name='initialview01'>2ez4</scene>, resolution 2.03&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Pyruvate_oxidase Pyruvate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.3.3 1.2.3.3]
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|GENE= pox5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1590 Lactobacillus plantarum])
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}}
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'''Pyruvate oxidase variant F479W'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2EZ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_plantarum Lactobacillus plantarum] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=TPP:'>TPP</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pyruvate_oxidase Pyruvate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.3.3 1.2.3.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZ4 OCA].
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2EZ4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_plantarum Lactobacillus plantarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZ4 OCA].
==Reference==
==Reference==
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The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography., Wille G, Meyer D, Steinmetz A, Hinze E, Golbik R, Tittmann K, Nat Chem Biol. 2006 Jun;2(6):324-8. Epub 2006 May 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16680160 16680160]
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The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography., Wille G, Meyer D, Steinmetz A, Hinze E, Golbik R, Tittmann K, Nat Chem Biol. 2006 Jun;2(6):324-8. Epub 2006 May 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16680160 16680160]
[[Category: Lactobacillus plantarum]]
[[Category: Lactobacillus plantarum]]
[[Category: Pyruvate oxidase]]
[[Category: Pyruvate oxidase]]
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[[Category: tpp enzyme]]
[[Category: tpp enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:15:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:46:04 2008''

Revision as of 14:46, 20 March 2008

Image:2ez4.gif


PDB ID 2ez4

Drag the structure with the mouse to rotate
, resolution 2.03Å
Ligands: , , , and
Gene: pox5 (Lactobacillus plantarum)
Activity: Pyruvate oxidase, with EC number 1.2.3.3
Coordinates: save as pdb, mmCIF, xml



Pyruvate oxidase variant F479W


Overview

Enzymes that use the cofactor thiamin diphosphate (ThDP, 1), the biologically active form of vitamin B(1), are involved in numerous metabolic pathways in all organisms. Although a theory of the cofactor's underlying reaction mechanism has been established over the last five decades, the three-dimensional structures of most major reaction intermediates of ThDP enzymes have remained elusive. Here, we report the X-ray structures of key intermediates in the oxidative decarboxylation of pyruvate, a central reaction in carbon metabolism catalyzed by the ThDP- and flavin-dependent enzyme pyruvate oxidase (POX)3 from Lactobacillus plantarum. The structures of 2-lactyl-ThDP (LThDP, 2) and its stable phosphonate analog, of 2-hydroxyethyl-ThDP (HEThDP, 3) enamine and of 2-acetyl-ThDP (AcThDP, 4; all shown bound to the enzyme's active site) provide profound insights into the chemical mechanisms and the stereochemical course of thiamin catalysis. These snapshots also suggest a mechanism for a phosphate-linked acyl transfer coupled to electron transfer in a radical reaction of pyruvate oxidase.

About this Structure

2EZ4 is a Single protein structure of sequence from Lactobacillus plantarum. Full crystallographic information is available from OCA.

Reference

The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography., Wille G, Meyer D, Steinmetz A, Hinze E, Golbik R, Tittmann K, Nat Chem Biol. 2006 Jun;2(6):324-8. Epub 2006 May 7. PMID:16680160

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