1g93: Difference between revisions

Revision as of 13:47, 21 February 2008

CRYSTAL STRUCTURE OF THE BOVINE CATALYTIC DOMAIN OF ALPHA-1,3-GALACTOSYLTRANSFERASE IN THE PRESENCE OF UDP-GALACTOSE

OverviewOverview

alpha1,3-galactosyltransferase (alpha3GalT, EC 2.4.1.151) is a Golgi-resident, type II transmembrane protein that transfers galactose from UDP-alpha-galactose to the terminal N:-acetyllactosamine unit of glycoconjugate glycans, producing the Galalpha1,3Galbeta1,4GlcNAc oligosaccharide structure present in most mammalian glycoproteins. Unlike most other mammals, humans and Old World primates do not possess alpha3GalT activity, which is relevant for the hyperacute rejection observed in pig-to-human xenotransplantation. The crystal structure of the catalytic domain of substrate-free bovine alpha3GalT, solved and refined to 2.3 A resolution, has a globular shape with an alpha/beta fold containing a narrow cleft on one face, and shares a UDP-binding domain (UBD) with the recently solved inverting glycosyltransferases. The substrate-bound complex, solved and refined to 2.5 A, allows the description of residues interacting directly with UDP-galactose. These structural data suggest that the strictly conserved residue E317 is likely to be the catalytic nucleophile involved in galactose transfer with retention of anomeric configuration as accomplished by this enzyme. Moreover, the alpha3GalT structure helps to identify amino acid residues that determine the specificities of the highly homologous ABO histo-blood group and glycosphingolipid glycosyltransferases.

About this StructureAbout this Structure

1G93 is a Single protein structure of sequence from Bos taurus with , , and as ligands. Active as N-acetyllactosaminide 3-alpha-galactosyltransferase, with EC number 2.4.1.87 Full crystallographic information is available from OCA.

ReferenceReference

Bovine alpha1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases., Gastinel LN, Bignon C, Misra AK, Hindsgaul O, Shaper JH, Joziasse DH, EMBO J. 2001 Feb 15;20(4):638-49. PMID:11179209

Page seeded by OCA on Thu Feb 21 12:47:29 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1g93.jpg|left|200px]]<br /><applet load="1g93" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1g93.jpg|left|200px]]<br /><applet load="1g93" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1g93, resolution 2.5&Aring;" />
 '''CRYSTAL STRUCTURE OF THE BOVINE CATALYTIC DOMAIN OF ALPHA-1,3-GALACTOSYLTRANSFERASE IN THE PRESENCE OF UDP-GALACTOSE'''<br />
 ==Overview==
-alpha1,3-galactosyltransferase (alpha3GalT, EC 2.4.1.151) is a, Golgi-resident, type II transmembrane protein that transfers galactose, from UDP-alpha-galactose to the terminal N:-acetyllactosamine unit of, glycoconjugate glycans, producing the Galalpha1,3Galbeta1,4GlcNAc, oligosaccharide structure present in most mammalian glycoproteins. Unlike, most other mammals, humans and Old World primates do not possess, alpha3GalT activity, which is relevant for the hyperacute rejection, observed in pig-to-human xenotransplantation. The crystal structure of the, catalytic domain of substrate-free bovine alpha3GalT, solved and refined, to 2.3 A resolution, has a globular shape with an alpha/beta fold, containing a narrow cleft on one face, and shares a UDP-binding domain, (UBD) with the recently solved inverting glycosyltransferases. The, substrate-bound complex, solved and refined to 2.5 A, allows the, description of residues interacting directly with UDP-galactose. These, structural data suggest that the strictly conserved residue E317 is likely, to be the catalytic nucleophile involved in galactose transfer with, retention of anomeric configuration as accomplished by this enzyme., Moreover, the alpha3GalT structure helps to identify amino acid residues, that determine the specificities of the highly homologous ABO histo-blood, group and glycosphingolipid glycosyltransferases.
+alpha1,3-galactosyltransferase (alpha3GalT, EC 2.4.1.151) is a Golgi-resident, type II transmembrane protein that transfers galactose from UDP-alpha-galactose to the terminal N:-acetyllactosamine unit of glycoconjugate glycans, producing the Galalpha1,3Galbeta1,4GlcNAc oligosaccharide structure present in most mammalian glycoproteins. Unlike most other mammals, humans and Old World primates do not possess alpha3GalT activity, which is relevant for the hyperacute rejection observed in pig-to-human xenotransplantation. The crystal structure of the catalytic domain of substrate-free bovine alpha3GalT, solved and refined to 2.3 A resolution, has a globular shape with an alpha/beta fold containing a narrow cleft on one face, and shares a UDP-binding domain (UBD) with the recently solved inverting glycosyltransferases. The substrate-bound complex, solved and refined to 2.5 A, allows the description of residues interacting directly with UDP-galactose. These structural data suggest that the strictly conserved residue E317 is likely to be the catalytic nucleophile involved in galactose transfer with retention of anomeric configuration as accomplished by this enzyme. Moreover, the alpha3GalT structure helps to identify amino acid residues that determine the specificities of the highly homologous ABO histo-blood group and glycosphingolipid glycosyltransferases.
 ==About this Structure==
-G93 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 GAL, MN, HG and UPG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/N-acetyllactosaminide_3-alpha-galactosyltransferase N-acetyllactosaminide 3-alpha-galactosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.87 2.4.1.87] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G93 OCA].
+G93 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=GAL:'>GAL</scene>, <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=HG:'>HG</scene> and <scene name='pdbligand=UPG:'>UPG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/N-acetyllactosaminide_3-alpha-galactosyltransferase N-acetyllactosaminide 3-alpha-galactosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.87 2.4.1.87] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G93 OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Bignon, C.]]
-[[Category: Gastinel, L.N.]]
+[[Category: Gastinel, L N.]]
 [[Category: Hindsgaul, O.]]
-[[Category: Joziasse, D.H.]]
+[[Category: Joziasse, D H.]]
-[[Category: Misra, A.K.]]
+[[Category: Misra, A K.]]
-[[Category: Shaper, J.H.]]
+[[Category: Shaper, J H.]]
 [[Category: GAL]]
 [[Category: HG]]
@@ Line 28: / Line 28: @@
 [[Category: udp binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:50:09 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:29 2008''