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New page: left|200px<br /><applet load="1pox" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pox, resolution 2.1Å" /> '''THE REFINED STRUCTURE...
 
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[[Image:1pox.gif|left|200px]]<br /><applet load="1pox" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1pox, resolution 2.1&Aring;" />
'''THE REFINED STRUCTURES OF A STABILIZED MUTANT AND OF WILD-TYPE PYRUVATE OXIDASE FROM LACTOBACILLUS PLANTARUM'''<br />


==Overview==
==THE REFINED STRUCTURES OF A STABILIZED MUTANT AND OF WILD-TYPE PYRUVATE OXIDASE FROM LACTOBACILLUS PLANTARUM==
The crystal structure of pyruvate oxidase (EC 1.2.3.3) from Lactobacillus, plantarum stabilized by three point mutations has been refined at 2.1 A, resolution using the simulated annealing method. Based on 87,775, independent reflections in the resolution range 10 to 2.1 A, a final, R-factor of 16.2% was obtained at good model geometry. The wild-type, enzyme crystallizes isomorphously with the stabilized enzyme and has been, analyzed at 2.5 A resolution. Pyruvate oxidase is a homotetramer with, point group symmetry D2. One 2-fold axis is crystallographic, the others, are local. The crystallographic asymmetric unit contains two subunits, and, the model consists of the two polypeptide chains (residues 9 through 593), two FAD, two ThDP*Mg2+ and 739 water molecules. Each subunit has three, domains; the CORE domain, the FAD domain and the ThDP domain. The, FAD-binding chain fold is different from those of other known, flavoproteins, whereas the ThDP-binding chain fold resembles the, corresponding folds of the two other ThDP enzymes whose structure is, known, transketolase and pyruvate decarboxylase. The peptide environment, most likely forces the pyrimidine ring of ThDP into an unusual tautomeric, form, which is required for catalysis. The structural differences between, the wild-type and the stabilized enzyme are small. All three point, mutations are at or near to the subunit interfaces, indicating that they, stabilize the quarternary structure as had been deduced from, reconstitution experiments.
<StructureSection load='1pox' size='340' side='right'caption='[[1pox]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1pox]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactiplantibacillus_plantarum Lactiplantibacillus plantarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1POX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1POX FirstGlance]. <br>
1POX 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 MG, NA, TPP, FAD and GOL 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1POX OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pox OCA], [https://pdbe.org/1pox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pox RCSB], [https://www.ebi.ac.uk/pdbsum/1pox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pox ProSAT]</span></td></tr>
The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum., Muller YA, Schumacher G, Rudolph R, Schulz GE, J Mol Biol. 1994 Apr 1;237(3):315-35. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8145244 8145244]
</table>
[[Category: Lactobacillus plantarum]]
== Function ==
[[Category: Pyruvate oxidase]]
[https://www.uniprot.org/uniprot/POXB_LACPL POXB_LACPL] Important for the aerobic growth. Decarboxylates pyruvate in four steps. The energy released is partially stored in acetyl phosphate.
[[Category: Single protein]]
== Evolutionary Conservation ==
[[Category: Muller, Y.A.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Schulz, G.E.]]
Check<jmol>
[[Category: FAD]]
  <jmolCheckbox>
[[Category: GOL]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/1pox_consurf.spt"</scriptWhenChecked>
[[Category: MG]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: NA]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: TPP]]
  </jmolCheckbox>
[[Category: oxidoreductase(oxygen as acceptor)]]
</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=1pox ConSurf].
 
<div style="clear:both"></div>
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:59:03 2007''
__TOC__
</StructureSection>
[[Category: Lactiplantibacillus plantarum]]
[[Category: Large Structures]]
[[Category: Muller YA]]
[[Category: Schulz GE]]

Latest revision as of 08:10, 14 February 2024

THE REFINED STRUCTURES OF A STABILIZED MUTANT AND OF WILD-TYPE PYRUVATE OXIDASE FROM LACTOBACILLUS PLANTARUM

1pox, resolution 2.10Å

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