4xim

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(New page: 200px<br /><applet load="4xim" size="450" color="white" frame="true" align="right" spinBox="true" caption="4xim, resolution 2.3&Aring;" /> '''PROTEIN ENGINEERING O...)
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[[Image:4xim.jpg|left|200px]]<br /><applet load="4xim" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="4xim, resolution 2.3&Aring;" />
 
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'''PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM ACTINOPLANES MISSOURIENSIS. 1. CRYSTALLOGRAPHY AND SITE-DIRECTED MUTAGENESIS OF METAL BINDING SITES'''<br />
 
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==Overview==
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==PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM ACTINOPLANES MISSOURIENSIS. 1. CRYSTALLOGRAPHY AND SITE-DIRECTED MUTAGENESIS OF METAL BINDING SITES==
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The structure and function of the xylose (glucose) isomerase from, Actinoplanes missouriensis have been analyzed by X-ray crystallography and, site-directed mutagenesis after cloning and overexpression in Escherichia, coli. The crystal structure of wild-type enzyme has been refined to an R, factor of 15.2% against diffraction data to 2.2-A resolution. The, structures of a number of binary and ternary complexes involving wild-type, and mutant enzymes, the divalent cations Mg2+, Co2+, or Mn2+, and either, the substrate xylose or substrate analogs have also been determined and, refined to comparable R factors. Two metal sites are identified. Metal, site 1 is four-coordinated and tetrahedral in the absence of substrate and, is six-coordinated and octahedral in its presence; the O2 and O4 atoms of, linear inhibitors and substrate bind to metal 1. Metal site 2 is, octahedral in all cases; its position changes by 0.7 A when it binds O1 of, the substrate and by more than 1 A when it also binds O2; these bonds, replace bonds to carboxylate ligands from the protein. Side chains, involved in metal binding have been substituted by site-directed, mutagenesis. The biochemical properties of the mutant enzymes are, presented. Together with structural data, they demonstrate that the two, metal ions play an essential part in binding substrates, in stabilizing, their open form, and in catalyzing hydride transfer between the C1 and C2, positions.
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<StructureSection load='4xim' size='340' side='right'caption='[[4xim]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4xim]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinoplanes_missouriensis Actinoplanes missouriensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XIM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XIM 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]] 2.3&#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=CO:COBALT+(II)+ION'>CO</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=4xim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xim OCA], [https://pdbe.org/4xim PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xim RCSB], [https://www.ebi.ac.uk/pdbsum/4xim PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xim ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/XYLA_ACTM4 XYLA_ACTM4]
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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/xi/4xim_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=4xim 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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4XIM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Actinoplanes_missouriensis Actinoplanes missouriensis] with CO as [http://en.wikipedia.org/wiki/ligand ligand]. 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=4XIM 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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Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 1. Crystallography and site-directed mutagenesis of metal binding sites., Jenkins J, Janin J, Rey F, Chiadmi M, van Tilbeurgh H, Lasters I, De Maeyer M, Van Belle D, Wodak SJ, Lauwereys M, et al., Biochemistry. 1992 Jun 23;31(24):5449-58. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1610791 1610791]
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[[Category: Actinoplanes missouriensis]]
[[Category: Actinoplanes missouriensis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Xylose isomerase]]
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[[Category: Janin J]]
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[[Category: Janin, J.]]
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[[Category: CO]]
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[[Category: isomerase(intramolecular oxidoreductse)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:51:52 2007''
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Current revision

PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM ACTINOPLANES MISSOURIENSIS. 1. CRYSTALLOGRAPHY AND SITE-DIRECTED MUTAGENESIS OF METAL BINDING SITES

PDB ID 4xim

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