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| | <StructureSection load='2nlx' size='340' side='right'caption='[[2nlx]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='2nlx' size='340' side='right'caption='[[2nlx]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2nlx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NLX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2nlx]] 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=2NLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NLX FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2itm|2itm]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">xylB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Xylulokinase Xylulokinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.17 2.7.1.17] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nlx OCA], [https://pdbe.org/2nlx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nlx RCSB], [https://www.ebi.ac.uk/pdbsum/2nlx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nlx ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nlx OCA], [https://pdbe.org/2nlx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nlx RCSB], [https://www.ebi.ac.uk/pdbsum/2nlx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nlx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/XYLB_ECOLI XYLB_ECOLI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Xylulokinase]]
| + | [[Category: Voegtli J]] |
| - | [[Category: Luccio, E di]]
| + | [[Category: Wilson DK]] |
| - | [[Category: Voegtli, J]] | + | [[Category: Di Luccio E]] |
| - | [[Category: Wilson, D K]] | + | |
| - | [[Category: Atpase]] | + | |
| - | [[Category: Fggy kinase]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Xylulose]]
| + | |
| Structural highlights
Function
XYLB_ECOLI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The primary metabolic route for D-xylose, the second most abundant sugar in nature, is via the pentose phosphate pathway after a two-step or three-step conversion to xylulose-5-phosphate. Xylulose kinase (XK; EC 2.7.1.17) phosphorylates D-xylulose, the last step in this conversion. The apo and D-xylulose-bound crystal structures of Escherichia coli XK have been determined and show a dimer composed of two domains separated by an open cleft. XK dimerization was observed directly by a cryo-EM reconstruction at 36 A resolution. Kinetic studies reveal that XK has a weak substrate-independent MgATP-hydrolyzing activity, and phosphorylates several sugars and polyols with low catalytic efficiency. Binding of pentulose and MgATP to form the reactive ternary complex is strongly synergistic. Although the steady-state kinetic mechanism of XK is formally random, a path is preferred in which D-xylulose binds before MgATP. Modelling of MgATP binding to XK and the accompanying conformational change suggests that sugar binding is accompanied by a dramatic hinge-bending movement that enhances interactions with MgATP, explaining the observed synergism. A catalytic mechanism is proposed and supported by relevant site-directed mutants.
Structural and kinetic studies of induced fit in xylulose kinase from Escherichia coli.,Di Luccio E, Petschacher B, Voegtli J, Chou HT, Stahlberg H, Nidetzky B, Wilson DK J Mol Biol. 2007 Jan 19;365(3):783-98. Epub 2006 Oct 25. PMID:17123542[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Di Luccio E, Petschacher B, Voegtli J, Chou HT, Stahlberg H, Nidetzky B, Wilson DK. Structural and kinetic studies of induced fit in xylulose kinase from Escherichia coli. J Mol Biol. 2007 Jan 19;365(3):783-98. Epub 2006 Oct 25. PMID:17123542 doi:10.1016/j.jmb.2006.10.068
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