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1xim

From Proteopedia

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[[Image:1xim.jpg|left|200px]]
 
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{{Structure
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==ARGININE RESIDUES AS STABILIZING ELEMENTS IN PROTEINS==
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|PDB= 1xim |SIZE=350|CAPTION= <scene name='initialview01'>1xim</scene>, resolution 2.2&Aring;
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<StructureSection load='1xim' size='340' side='right'caption='[[1xim]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=XYL:D-XYLITOL'>XYL</scene> and <scene name='pdbligand=CO:COBALT (II) ION'>CO</scene>
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<table><tr><td colspan='2'>[[1xim]] 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=1XIM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XIM FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 2.2&#8491;</td></tr>
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|GENE=
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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>, <scene name='pdbligand=XYL:D-XYLITOL'>XYL</scene></td></tr>
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}}
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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=1xim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xim OCA], [https://pdbe.org/1xim PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xim RCSB], [https://www.ebi.ac.uk/pdbsum/1xim PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xim 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/1xim_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=1xim ConSurf].
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<div style="clear:both"></div>
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'''ARGININE RESIDUES AS STABILIZING ELEMENTS IN PROTEINS'''
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==See Also==
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*[[D-xylose isomerase 3D structures|D-xylose isomerase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Site-specific substitutions of arginine for lysine in the thermostable D-xylose isomerase (XI) from Actinoplanes missouriensis are shown to impart significant heat stability enhancement in the presence of sugar substrates most probably by interfering with nonenzymatic glycation. The same substitutions are also found to increase heat stability in the absence of any sugar derivatives, where a mechanism based on prevention of glycation can no longer be invoked. This rather conservative substitution is moreover shown to improve thermostability in two other structurally unrelated proteins, human copper, zinc-superoxide dismutase (CuZnSOD) and D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Bacillus subtilis. The stabilizing effect of Lys----Arg substitutions is rationalized on the basis of a detailed analysis of the crystal structures of wild-type XI and of engineered variants with Lys----Arg substitution at four distinct locations, residues 253, 309, 319, and 323. Molecular model building analysis of the structures of wild-type and mutant CuZnSOD (K9R) and GAPDH (G281K and G281R) is used to explain the observed stability enhancement in these proteins. In addition to demonstrating that even thermostable proteins can lend themselves to further stability improvement, our findings provide direct evidence that arginine residues are important stabilizing elements in proteins. Moreover, the stabilizing role of electrostatic interactions, particularly between subunits in oligomeric proteins, is documented.
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==About this Structure==
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1XIM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Actinoplanes_missouriensis Actinoplanes missouriensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XIM OCA].
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==Reference==
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Arginine residues as stabilizing elements in proteins., Mrabet NT, Van den Broeck A, Van den brande I, Stanssens P, Laroche Y, Lambeir AM, Matthijssens G, Jenkins J, Chiadmi M, van Tilbeurgh H, et al., Biochemistry. 1992 Mar 3;31(8):2239-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1540579 1540579]
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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: Chiadmi M]]
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[[Category: Brande, I Van Den.]]
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[[Category: Demaeyer M]]
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[[Category: Chiadmi, M.]]
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[[Category: Janin J]]
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[[Category: Demaeyer, M.]]
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[[Category: Jenkins J]]
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[[Category: Denbroek, A Van.]]
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[[Category: Lambeir A-M]]
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[[Category: Janin, J.]]
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[[Category: Laroche Y]]
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[[Category: Jenkins, J.]]
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[[Category: Lasters I]]
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[[Category: Lambeir, A M.]]
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[[Category: Matthyssens G]]
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[[Category: Laroche, Y.]]
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[[Category: Mrabet NT]]
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[[Category: Lasters, I.]]
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[[Category: Quax WJ]]
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[[Category: Matthyssens, G.]]
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[[Category: Rey F]]
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[[Category: Mrabet, N T.]]
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[[Category: Stanssens P]]
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[[Category: Quax, W J.]]
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[[Category: Van Den Brande I]]
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[[Category: Rey, F.]]
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[[Category: Van Denbroek A]]
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[[Category: Stanssens, P.]]
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[[Category: Vantilbeurgh H]]
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[[Category: Vantilbeurgh, H.]]
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[[Category: Wodak SJ]]
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[[Category: Wodak, S J.]]
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[[Category: CO]]
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[[Category: XYL]]
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[[Category: isomerase(intramolecular oxidoreductse)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:10:19 2008''
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Current revision

ARGININE RESIDUES AS STABILIZING ELEMENTS IN PROTEINS

PDB ID 1xim

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