2agd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:2agd.gif|left|200px]]
[[Image:2agd.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 2agd |SIZE=350|CAPTION= <scene name='initialview01'>2agd</scene>, resolution 1.90&Aring;
+
The line below this paragraph, containing "STRUCTURE_2agd", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6-AMINOHEXYL-URIDINE-C1,5&#39;-DIPHOSPHATE'>UDH</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetyllactosamine_synthase N-acetyllactosamine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.90 2.4.1.90] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE= B4GALT1, GGTB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_2agd| PDB=2agd | SCENE= }}
-
|RELATEDENTRY=[[1o0r|1O0R]], [[1tvy|1TVY]], [[1tw1|1TW1]], [[1tw5|1TW5]]
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2agd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2agd OCA], [http://www.ebi.ac.uk/pdbsum/2agd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2agd RCSB]</span>
+
-
}}
+
'''Crystal Structure of Human M340H-Beta-1,4-Galactosyltransferase-I(M340H-B4Gal-T1) in Complex with GlcNAc-beta1,4-Man-alpha1,3-Man-beta-OR'''
'''Crystal Structure of Human M340H-Beta-1,4-Galactosyltransferase-I(M340H-B4Gal-T1) in Complex with GlcNAc-beta1,4-Man-alpha1,3-Man-beta-OR'''
Line 32: Line 29:
[[Category: Ratner, D M.]]
[[Category: Ratner, D M.]]
[[Category: Seeberger, P H.]]
[[Category: Seeberger, P H.]]
-
[[Category: beta1,4-galactosyltransferase-i]]
+
[[Category: Beta1,4-galactosyltransferase-i]]
-
[[Category: closed conformation]]
+
[[Category: Closed conformation]]
-
[[Category: mutant]]
+
[[Category: Mutant]]
-
[[Category: trisaccharide]]
+
[[Category: Trisaccharide]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:01:02 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:52:17 2008''
+

Revision as of 16:01, 3 May 2008

Template:STRUCTURE 2agd

Crystal Structure of Human M340H-Beta-1,4-Galactosyltransferase-I(M340H-B4Gal-T1) in Complex with GlcNAc-beta1,4-Man-alpha1,3-Man-beta-OR


Overview

beta-1,4-Galactosyltransferase-I (beta4Gal-T1) transfers galactose from UDP-galactose to N-acetylglucosamine (GlcNAc) residues of the branched N-linked oligosaccharide chains of glycoproteins. In an N-linked biantennary oligosaccharide chain, one antenna is attached to the 3-hydroxyl-(1,3-arm), and the other to the 6-hydroxyl-(1,6-arm) group of mannose, which is beta-1,4-linked to an N-linked chitobiose, attached to the aspargine residue of a protein. For a better understanding of the branch specificity of beta4Gal-T1 towards the GlcNAc residues of N-glycans, we have carried out kinetic and crystallographic studies with the wild-type human beta4Gal-T1 (h-beta4Gal-T1) and the mutant Met340His-beta4Gal-T1 (h-M340H-beta4Gal-T1) in complex with a GlcNAc-containing pentasaccharide and several GlcNAc-containing trisaccharides present in N-glycans. The oligosaccharides used were: pentasaccharide GlcNAcbeta1,2-Manalpha1,6 (GlcNAcbeta1,2-Manalpha1,3)Man; the 1,6-arm trisaccharide, GlcNAcbeta1,2-Manalpha1,6-Manbeta-OR (1,2-1,6-arm); the 1,3-arm trisaccharides, GlcNAcbeta1,2-Manalpha1,3-Manbeta-OR (1,2-1,3-arm) and GlcNAcbeta1,4-Manalpha1,3-Manbeta-OR (1,4-1,3-arm); and the trisaccharide GlcNAcbeta1,4-GlcNAcbeta1,4-GlcNAc (chitotriose). With the wild-type h-beta4Gal-T1, the K(m) of 1,2-1,6-arm is approximately tenfold lower than for 1,2-1,3-arm and 1,4-1,3-arm, and 22-fold lower than for chitotriose. Crystal structures of h-M340H-beta4Gal-T1 in complex with the pentasaccharide and various trisaccharides at 1.9-2.0A resolution showed that beta4Gal-T1 is in a closed conformation with the oligosaccharide bound to the enzyme, and the 1,2-1,6-arm trisaccharide makes the maximum number of interactions with the enzyme, which is in concurrence with the lowest K(m) for the trisaccharide. Present studies suggest that beta4Gal-T1 interacts preferentially with the 1,2-1,6-arm trisaccharide rather than with the 1,2-1,3-arm or 1,4-1,3-arm of a bi- or tri-antennary oligosaccharide chain of N-glycan.

About this Structure

2AGD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Oligosaccharide preferences of beta1,4-galactosyltransferase-I: crystal structures of Met340His mutant of human beta1,4-galactosyltransferase-I with a pentasaccharide and trisaccharides of the N-glycan moiety., Ramasamy V, Ramakrishnan B, Boeggeman E, Ratner DM, Seeberger PH, Qasba PK, J Mol Biol. 2005 Oct 14;353(1):53-67. PMID:16157350 Page seeded by OCA on Sat May 3 19:01:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools