1ucw

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[[Image:1ucw.jpg|left|200px]]
[[Image:1ucw.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1ucw |SIZE=350|CAPTION= <scene name='initialview01'>1ucw</scene>, resolution 2.2&Aring;
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The line below this paragraph, containing "STRUCTURE_1ucw", 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= <scene name='pdbligand=LLY:NZ-(DICARBOXYMETHYL)LYSINE'>LLY</scene>
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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/Transaldolase Transaldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1ucw| PDB=1ucw | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ucw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ucw OCA], [http://www.ebi.ac.uk/pdbsum/1ucw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ucw RCSB]</span>
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}}
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'''COMPLEX OF TRANSALDOLASE WITH THE REDUCED SCHIFF-BASE INTERMEDIATE'''
'''COMPLEX OF TRANSALDOLASE WITH THE REDUCED SCHIFF-BASE INTERMEDIATE'''
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[[Category: Lindqvist, Y.]]
[[Category: Lindqvist, Y.]]
[[Category: Schneider, G.]]
[[Category: Schneider, G.]]
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[[Category: ketone residue]]
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[[Category: Ketone residue]]
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[[Category: pentose shunt]]
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[[Category: Pentose shunt]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:03:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:08:34 2008''
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Revision as of 08:03, 3 May 2008

Image:1ucw.jpg

Template:STRUCTURE 1ucw

COMPLEX OF TRANSALDOLASE WITH THE REDUCED SCHIFF-BASE INTERMEDIATE


Overview

Transaldolase catalyzes transfer of a dihydroxyacetone moiety from a ketose donor to an aldose acceptor. During catalysis, a Schiff-base intermediate between dihydroxyacetone and the epsilon-amino group of a lysine residue at the active site of the enzyme is formed. This Schiff-base intermediate has been trapped by reduction with potassium borohydride, and the crystal structure of this complex has been determined at 2.2 A resolution. The overall structures of the complex and the native enzyme are very similar; formation of the intermediate induces no large conformational changes. The dihydroxyacetone moiety is covalently linked to the side chain of Lys 132 at the active site of the enzyme. The Cl hydroxyl group of the dihydroxyacetone moiety forms hydrogen bonds to the side chains of residues Asn 154 and Ser 176. The C3 hydroxyl group interacts with the side chain of Asp 17 and Asn 35. Based on the crystal structure of this complex a reaction mechanism for transaldolase is proposed.

About this Structure

1UCW is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: mechanistic implications for class I aldolases., Jia J, Schorken U, Lindqvist Y, Sprenger GA, Schneider G, Protein Sci. 1997 Jan;6(1):119-24. PMID:9007983 Page seeded by OCA on Sat May 3 11:03:15 2008

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