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1xyl

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(New page: 200px<br /><applet load="1xyl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xyl, resolution 1.8&Aring;" /> '''THE ROLE OF THE DIVAL...)
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[[Image:1xyl.gif|left|200px]]<br /><applet load="1xyl" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1xyl, resolution 1.8&Aring;" />
 
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'''THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID'''<br />
 
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==Overview==
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==THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID==
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The distinct roles of the two magnesium ions essential to the activity of, D-xylose isomerase from Streptomyces olivochromogenes were examined. The, enzyme-magnesium complex was isolated, and the stoichiometry of cation, binding determined by neutron activation analysis to be 2 mol of magnesium, per mole of enzyme. A plot of Mg2+ added versus Mg2+ bound to enzyme is, consistent with apparent KD values of &lt; or = 0.5-1.0 mM for one Mg2+ and &lt;, or = 2-5 mM for the second. A site-directed mutant of D-xylose isomerase, was designed to remove the tighter, tetracoordinated magnesium binding, site (site 1, Mg-1); Glu180 was replaced with Lys180. The stoichiometry of, metal binding to this mutant, E180K, is 1 mol of magnesium per mole of, enzyme. Ring-opening assays with 1-thioglucose (H2S released upon ring, opening) show E180K catalyzes the opening of the sugar ring at 20% the, rate of the wild-type, but E180K does not catalyze isomerization of, glucose to fructose. Thus, the magnesium bound to Glu180 is essential for, isomerization but not essential for ring opening. The X-ray, crystallographic structures of E180K in the absence of magnesium and in, the presence and absence of 250 mM glucose were obtained to 1.8-A, resolution and refined to R factors of 17.7% and 19.7%, respectively. The, wild-type and both E180K structures show no significant structural, differences, except the epsilon-amino group of Lys180, which occupies the, position usually occupied by the Mg-1.(ABSTRACT TRUNCATED AT 250 WORDS)
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<StructureSection load='1xyl' size='340' side='right'caption='[[1xyl]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1xyl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_olivochromogenes Streptomyces olivochromogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XYL FirstGlance]. <br>
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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=OH:HYDROXIDE+ION'>OH</scene></td></tr>
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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=1xyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xyl OCA], [https://pdbe.org/1xyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xyl RCSB], [https://www.ebi.ac.uk/pdbsum/1xyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xyl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/XYLA_STROL XYLA_STROL] Involved in D-xylose catabolism.
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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/xy/1xyl_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=1xyl ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1XYL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_olivochromogenes Streptomyces olivochromogenes] with MG and OH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XYL OCA].
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*[[D-xylose isomerase 3D structures|D-xylose isomerase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acid., Allen KN, Lavie A, Glasfeld A, Tanada TN, Gerrity DP, Carlson SC, Farber GK, Petsko GA, Ringe D, Biochemistry. 1994 Feb 15;33(6):1488-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7906142 7906142]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Streptomyces olivochromogenes]]
[[Category: Streptomyces olivochromogenes]]
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[[Category: Xylose isomerase]]
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[[Category: Allen KN]]
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[[Category: Allen, K.N.]]
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[[Category: Lavie A]]
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[[Category: Lavie, A.]]
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[[Category: Petsko GA]]
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[[Category: Petsko, G.A.]]
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[[Category: Ringe D]]
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[[Category: Ringe, D.]]
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[[Category: MG]]
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[[Category: OH]]
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[[Category: isomerase(intramolecular oxidoreductase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:26:18 2007''
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Current revision

THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID

PDB ID 1xyl

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