2nlx

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[[Image:2nlx.gif|left|200px]]
[[Image:2nlx.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2nlx |SIZE=350|CAPTION= <scene name='initialview01'>2nlx</scene>, resolution 2.70&Aring;
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The line below this paragraph, containing "STRUCTURE_2nlx", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Xylulokinase Xylulokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.17 2.7.1.17] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= xylB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_2nlx| PDB=2nlx | SCENE= }}
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|RELATEDENTRY=[[2itm|2ITM]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nlx OCA], [http://www.ebi.ac.uk/pdbsum/2nlx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nlx RCSB]</span>
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}}
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'''Crystal structure of the apo E. coli xylulose kinase'''
'''Crystal structure of the apo E. coli xylulose kinase'''
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[[Category: Voegtli, J.]]
[[Category: Voegtli, J.]]
[[Category: Wilson, D K.]]
[[Category: Wilson, D K.]]
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[[Category: atpase]]
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[[Category: Atpase]]
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[[Category: fggy kinase]]
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[[Category: Fggy kinase]]
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[[Category: kinase]]
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[[Category: Kinase]]
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[[Category: xylulokinase]]
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[[Category: Xylulokinase]]
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[[Category: xylulose]]
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[[Category: Xylulose]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:37:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:05:02 2008''
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Revision as of 06:37, 4 May 2008

Image:2nlx.gif

Template:STRUCTURE 2nlx

Crystal structure of the apo E. coli xylulose kinase


Overview

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.

About this Structure

2NLX is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 09:37:28 2008

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