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1gx4
From Proteopedia
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| - | [[Image:1gx4.gif|left|200px]]<br /><applet load="1gx4" size=" | + | [[Image:1gx4.gif|left|200px]]<br /><applet load="1gx4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gx4, resolution 1.46Å" /> | caption="1gx4, resolution 1.46Å" /> | ||
'''ALPHA-,1,3 GALACTOSYLTRANSFERASE- N-ACETYL LACTOSAMINE COMPLEX'''<br /> | '''ALPHA-,1,3 GALACTOSYLTRANSFERASE- N-ACETYL LACTOSAMINE COMPLEX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MN, UDP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_2.4.1.87 Transferred entry: 2.4.1.87], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.151 2.4.1.151] Known structural/functional Site: <scene name='pdbsite=AC1:Nag Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1GX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=UDP:'>UDP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_2.4.1.87 Transferred entry: 2.4.1.87], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.151 2.4.1.151] Known structural/functional Site: <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GX4 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 Sun Feb 3 09:43:44 2008'' |
Revision as of 07:43, 3 February 2008
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ALPHA-,1,3 GALACTOSYLTRANSFERASE- N-ACETYL LACTOSAMINE COMPLEX
Overview
Bovine alpha-1,3-galactosyltransferase (alpha3GT) catalyzes the synthesis, of the alpha-galactose (alpha-Gal) epitope, the target of natural human, antibodies. It represents a family of enzymes, including the histo blood, group A and B transferases, that catalyze retaining glycosyltransfer, reactions of unknown mechanism. An initial study of alpha3GT in a crystal, form with limited resolution and considerable disorder suggested the, possible formation of a beta-galactosyl-enzyme covalent intermediate, (Gastinel, L. N., Bignon, C., Misra, A. K., Hindsgaul, O., Shaper, J. H., and Joziasse, D. H. (2001) EMBO J. 20, 638-649). Highly ordered structures, are described for complexes of alpha3GT with donor substrate, UDP-galactose, UDP- glucose, and two acceptor substrates, lactose and, N-acetyllactosamine, at resolutions up to 1.46 A. Structural and, calorimetric binding studies suggest an obligatory ordered binding of, donor and acceptor substrates, linked to a donor substrate-induced, conformational change, and the direct participation of UDP in acceptor, binding. The monosaccharide-UDP bond is cleaved in the structures, containing UDP-galactose and UDP-glucose, producing non-covalent complexes, containing buried beta-galactose and alpha-glucose. The location of these, monosaccharides and molecular modeling suggest that binding of a distorted, conformation of UDP-galactose may be important in the catalytic mechanism, of alpha3GT.
About this Structure
1GX4 is a Single protein structure of sequence from Bos taurus with , and as ligands. Active as Transferred entry: 2.4.1.87, with EC number 2.4.1.151 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase, alpha-1,3-galactosyltransferase., Boix E, Zhang Y, Swaminathan GJ, Brew K, Acharya KR, J Biol Chem. 2002 Aug 2;277(31):28310-8. Epub 2002 May 14. PMID:12011052
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