2ezu

From Proteopedia

(Difference between revisions)

Revision as of 07:31, 18 October 2017

Pyruvate oxidase variant F479W in complex with reaction intermediate 2-acetyl-thiamin diphosphate

Structural highlights

2ezu is a 2 chain structure with sequence from "lactobacillus_arabinosus"_fred_et_al. "lactobacillus arabinosus" fred et al.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	1pow, 1pox, 1y9d, 2ez4, 2ez8, 2ez9, 2ezt
Gene:	pox5 ("Lactobacillus arabinosus" Fred et al.)
Activity:	Pyruvate oxidase, with EC number 1.2.3.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[POXB_LACPL] Important for the aerobic growth. Decarboxylates pyruvate in four steps. The energy released is partially stored in acetyl phosphate.

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

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wille G, Meyer D, Steinmetz A, Hinze E, Golbik R, Tittmann K. The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography. Nat Chem Biol. 2006 Jun;2(6):324-8. Epub 2006 May 7. PMID:16680160 doi:http://dx.doi.org/10.1038/nchembio788

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ezu"

@@ Line 1: / Line 1: @@
 ==Pyruvate oxidase variant F479W in complex with reaction intermediate 2-acetyl-thiamin diphosphate==
 <StructureSection load='2ezu' size='340' side='right' caption='[[2ezu]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pox5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1590 "Lactobacillus arabinosus" Fred et al.])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=2ezu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ezu OCA], [http://pdbe.org/2ezu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ezu RCSB], [http://www.ebi.ac.uk/pdbsum/2ezu 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=2ezu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ezu OCA], [http://pdbe.org/2ezu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ezu RCSB], [http://www.ebi.ac.uk/pdbsum/2ezu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ezu ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2ezu ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

2ezu

From Proteopedia

Revision as of 07:31, 18 October 2017

Pyruvate oxidase variant F479W in complex with reaction intermediate 2-acetyl-thiamin diphosphate

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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