1ucw
From Proteopedia
(New page: 200px<br /><applet load="1ucw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ucw, resolution 2.2Å" /> '''COMPLEX OF TRANSALDOL...) |
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| - | [[Image:1ucw.jpg|left|200px]]<br /><applet load="1ucw" size=" | + | [[Image:1ucw.jpg|left|200px]]<br /><applet load="1ucw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ucw, resolution 2.2Å" /> | caption="1ucw, resolution 2.2Å" /> | ||
'''COMPLEX OF TRANSALDOLASE WITH THE REDUCED SCHIFF-BASE INTERMEDIATE'''<br /> | '''COMPLEX OF TRANSALDOLASE WITH THE REDUCED SCHIFF-BASE INTERMEDIATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Transaldolase catalyzes transfer of a dihydroxyacetone moiety from a | + | 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== | ==About this Structure== | ||
| - | 1UCW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http:// | + | 1UCW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UCW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:11 2008'' |
Revision as of 13:23, 21 February 2008
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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. Active as Transaldolase, with EC number 2.2.1.2 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
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