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| - | [[Image:1bxb.gif|left|200px]] | |
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| - | {{Structure
| + | ==XYLOSE ISOMERASE FROM THERMUS THERMOPHILUS== |
| - | |PDB= 1bxb |SIZE=350|CAPTION= <scene name='initialview01'>1bxb</scene>, resolution 2.2Å
| + | <StructureSection load='1bxb' size='340' side='right'caption='[[1bxb]], [[Resolution|resolution]] 2.20Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND=
| + | <table><tr><td colspan='2'>[[1bxb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BXB FirstGlance]. <br> |
| - | |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]
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | |GENE= XYLA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bxb OCA], [https://pdbe.org/1bxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bxb RCSB], [https://www.ebi.ac.uk/pdbsum/1bxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bxb ProSAT]</span></td></tr> |
| - | }}
| + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/XYLA_THET8 XYLA_THET8] |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bx/1bxb_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </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=1bxb ConSurf]. |
| | + | <div style="clear:both"></div> |
| | | | |
| - | '''XYLOSE ISOMERASE FROM THERMUS THERMOPHILUS'''
| + | ==See Also== |
| - | | + | *[[D-xylose isomerase 3D structures|D-xylose isomerase 3D structures]] |
| - | | + | __TOC__ |
| - | ==Overview== | + | </StructureSection> |
| - | The crystal structures of highly thermostable xylose isomerases from Thermus thermophilus (TthXI) and Thermus caldophilus (TcaXI), both with the optimum reaction temperature of 90 degrees C, have been determined by X-ray crystallography. The model of TcaXI has been refined to an R-factor of 17.8 % for data extending to 2.3 A and that of TthXI to 17.1 % for data extending to 2.2 A. The tetrameric arrangement of subunits characterized by the 222-symmetry and the tertiary fold of each subunit in both TcaXI and TthXI are basically the same as in other xylose isomerases. Each monomer is composed of two domains. Domain I (residues 1 to 321) folds into the (beta/alpha)8-barrel. Domain II (residues 322 to 387), lacking beta-strands, makes extensive contacts with domain I of an adjacent subunit. Each monomer of TcaXI contains ten beta-strands, 15 alpha-helices, and six 310-helices, while that of TthXI contains ten beta-strands, 16 alpha-helices, and five 310-helices. Although the electron density does not indicate the presence of bound metal ions in the present models of both TcaXI and TthXI, the active site residues show the conserved structural features. In order to understand the structural basis for thermostability of these enzymes, their structures have been compared with less thermostable XIs from Arthrobacter B3728 and Actinoplanes missouriensis (AXI and AmiXI), with the optimum reaction temperatures of 80 degrees C and 75 degrees C, respectively. Analyses of various factors that may affect protein thermostability indicate that the possible structural determinants of the enhanced thermostability of TcaXI/TthXI over AXI/AmiXI are (i) an increase in ion pairs and ion-pair networks, (ii) a decrease in the large inter-subunit cavities, (iii) a removal of potential deamidation/isoaspartate formation sites, and (iv) a shortened loop.
| + | [[Category: Large Structures]] |
| - | | + | [[Category: Thermus thermophilus HB8]] |
| - | ==About this Structure==
| + | [[Category: Chang C]] |
| - | 1BXB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BXB OCA].
| + | [[Category: Lee D-S]] |
| - | | + | [[Category: Park BC]] |
| - | ==Reference==
| + | [[Category: Suh SW]] |
| - | Crystal structures of thermostable xylose isomerases from Thermus caldophilus and Thermus thermophilus: possible structural determinants of thermostability., Chang C, Park BC, Lee DS, Suh SW, J Mol Biol. 1999 May 14;288(4):623-34. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10329168 10329168]
| + | |
| - | [[Category: Single protein]] | + | |
| - | [[Category: Thermus thermophilus]] | + | |
| - | [[Category: Xylose isomerase]]
| + | |
| - | [[Category: Chang, C.]] | + | |
| - | [[Category: Lee, D S.]] | + | |
| - | [[Category: Park, B C.]] | + | |
| - | [[Category: Suh, S W.]] | + | |
| - | [[Category: isomerase]]
| + | |
| - | [[Category: xylose metabolism]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:17:00 2008''
| + | |
