1xby

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[[Image:1xby.gif|left|200px]]
 
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==Structure of 3-keto-L-gulonate 6-phosphate decarboxylase E112D/T169A mutant with bound D-ribulose 5-phosphate==
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The line below this paragraph, containing "STRUCTURE_1xby", creates the "Structure Box" on the page.
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<StructureSection load='1xby' size='340' side='right'caption='[[1xby]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1xby]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XBY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XBY FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5RP:RIBULOSE-5-PHOSPHATE'>5RP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_1xby| PDB=1xby | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xby OCA], [https://pdbe.org/1xby PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xby RCSB], [https://www.ebi.ac.uk/pdbsum/1xby PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xby ProSAT]</span></td></tr>
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</table>
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'''Structure of 3-keto-L-gulonate 6-phosphate decarboxylase E112D/T169A mutant with bound D-ribulose 5-phosphate'''
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== Function ==
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[https://www.uniprot.org/uniprot/ULAD_ECOLI ULAD_ECOLI] Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization.<ref>PMID:11741871</ref>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-hex-3-ulose 6-phosphate synthase (HPS), members of the orotidine 5'-monophosphate decarboxylase (OMPDC) suprafamily, catalyze reactions that involve the formation of Mg(2+)-ion stabilized 1,2-enediolate intermediates. The active sites of KGPDC and HPS share several conserved residues, including the presumed ligands for the Mg(2+) and a catalytic histidine residue that has been implicated in protonation of the intermediate in the KGPDC-catalyzed reaction. As reported in the previous manuscript, both enzymes are naturally promiscuous, with KGPDC from Escherichia coli catalyzing a low level of the HPS reaction and the HPS from Methylomonas aminofaciens catalyzing a significant level of the KGPDC reaction. Interestingly, the promiscuous HPS reaction catalyzed by KGPDC can be significantly enhanced by replacing no more than four active site residues from KGPDC reaction with residues from HPS. In this manuscript, we report structural studies of wild-type and mutant KDGPC's that provide a structural explanation for both the natural promiscuity for the HPS reaction and the enhanced HPS activity and diminished KGPDC activity catalyzed by active site mutants.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xb/1xby_consurf.spt"</scriptWhenChecked>
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XBY OCA].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase., Wise EL, Yew WS, Akana J, Gerlt JA, Rayment I, Biochemistry. 2005 Feb 15;44(6):1816-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15697207 15697207]
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</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=1xby ConSurf].
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[[Category: Akana, J.]]
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<div style="clear:both"></div>
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[[Category: Gerlt, J A.]]
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== References ==
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[[Category: Rayment, I.]]
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<references/>
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[[Category: Wise, E L.]]
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__TOC__
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[[Category: Yew, W S.]]
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</StructureSection>
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[[Category: Tim barrel]]
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[[Category: Escherichia coli]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:50:01 2008''
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[[Category: Large Structures]]
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[[Category: Akana J]]
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[[Category: Gerlt JA]]
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[[Category: Rayment I]]
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[[Category: Wise EL]]
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[[Category: Yew WS]]

Current revision

Structure of 3-keto-L-gulonate 6-phosphate decarboxylase E112D/T169A mutant with bound D-ribulose 5-phosphate

PDB ID 1xby

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