1so5

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(New page: 200px<br /><applet load="1so5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1so5, resolution 1.80&Aring;" /> '''Crystal structure of...)
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[[Image:1so5.gif|left|200px]]<br /><applet load="1so5" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1so5, resolution 1.80&Aring;" />
 
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'''Crystal structure of E112Q mutant of 3-keto-L-gulonate 6-phosphate decarboxylase with bound L-threonohydroxamate 4-phosphate'''<br />
 
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==Overview==
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==Crystal structure of E112Q mutant of 3-keto-L-gulonate 6-phosphate decarboxylase with bound L-threonohydroxamate 4-phosphate==
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3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC), a member of the, orotidine monophosphate decarboxylase (OMPDC) suprafamily, catalyzes the, Mg(2+)-dependent decarboxylation of 3-keto-L-gulonate 6-phosphate to, L-xylulose 5-phosphate. Structural and biochemical evidence suggests that, the KGPDC reaction proceeds via a Mg(2+)-stabilized 1,2-cis-enediolate, intermediate. Protonation of the enediolate intermediate occurs in a, nonstereospecific manner to form L-xylulose 5-phosphate. Although the, exact mechanism of proton delivery is not known, Glu112, His136, and, Arg139 have been implicated in this process [Yew, W. S., Wise, E., Rayment, I., and Gerlt, J. A. (2004) Biochemistry 43, 6427-6437]., Surprisingly, single amino acid substitutions of these positions do not, substantially reduce catalytic activity but rather alter the, stereochemical course of the reaction. Here, we report the X-ray crystal, structures of four mutants, K64A, H136A, E112Q, and E112Q/H136A, each, determined in the presence of L-threonohydroxamate 4-phosphate, an, analogue of the enediolate intermediate, to 1.7, 1.9, 1.8, and 1.9 A, resolution, respectively. These structures reveal that substitutions of, Lys64, Glu112, and His136 cause changes in the positions of the, intermediate analogue and two active site water molecules that were, previously identified as possible proton donors. These changes correlate, with the observed alterations in the reaction stereochemistry for these, mutants, thereby supporting a reaction mechanism in which water molecules, competitively shuttle protons from the side chains of His136 and Arg139 to, alternate faces of the cis-enediolate intermediate. These studies further, underscore the wide variation in the reaction mechanisms in the OMPDC, suprafamily.
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<StructureSection load='1so5' size='340' side='right'caption='[[1so5]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1so5]] 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=1SO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SO5 FirstGlance]. <br>
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1SO5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG and TX4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SO5 OCA].
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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]] 1.8&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TX4:L-THREONOHYDROXAMATE+4-PHOSPHATE'>TX4</scene></td></tr>
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==Reference==
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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=1so5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1so5 OCA], [https://pdbe.org/1so5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1so5 RCSB], [https://www.ebi.ac.uk/pdbsum/1so5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1so5 ProSAT]</span></td></tr>
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Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: crystallographic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase., Wise EL, Yew WS, Gerlt JA, Rayment I, Biochemistry. 2004 Jun 1;43(21):6438-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15157078 15157078]
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</table>
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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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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/so/1so5_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=1so5 ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Gerlt, J.A.]]
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[[Category: Gerlt JA]]
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[[Category: Rayment, I.]]
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[[Category: Rayment I]]
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[[Category: Wise, E.L.]]
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[[Category: Wise EL]]
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[[Category: Yew, W.S.]]
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[[Category: Yew WS]]
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[[Category: MG]]
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[[Category: TX4]]
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[[Category: tim barrel; beta barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:31:19 2007''
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Current revision

Crystal structure of E112Q mutant of 3-keto-L-gulonate 6-phosphate decarboxylase with bound L-threonohydroxamate 4-phosphate

PDB ID 1so5

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