1v83

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|PDB= 1v83 |SIZE=350|CAPTION= <scene name='initialview01'>1v83</scene>, resolution 1.9&Aring;
|PDB= 1v83 |SIZE=350|CAPTION= <scene name='initialview01'>1v83</scene>, resolution 1.9&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene> and <scene name='pdbligand=UDP:URIDINE-5&#39;-DIPHOSPHATE'>UDP</scene>
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=UDP:URIDINE-5&#39;-DIPHOSPHATE'>UDP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Galactosylgalactosylxylosylprotein_3-beta-glucuronosyltransferase Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.135 2.4.1.135]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactosylgalactosylxylosylprotein_3-beta-glucuronosyltransferase Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.135 2.4.1.135] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1v82|1V82]], [[1v84|1V84]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v83 OCA], [http://www.ebi.ac.uk/pdbsum/1v83 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v83 RCSB]</span>
}}
}}
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[[Category: Tagawa, H.]]
[[Category: Tagawa, H.]]
[[Category: Wakatsuki, S.]]
[[Category: Wakatsuki, S.]]
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[[Category: MN]]
 
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[[Category: TLA]]
 
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[[Category: UDP]]
 
[[Category: glycocyltransferase]]
[[Category: glycocyltransferase]]
[[Category: glycoprotein]]
[[Category: glycoprotein]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:58:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:20:42 2008''

Revision as of 21:20, 30 March 2008


PDB ID 1v83

Drag the structure with the mouse to rotate
, resolution 1.9Å
Ligands: , ,
Activity: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase, with EC number 2.4.1.135
Related: 1V82, 1V84


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of human GlcAT-P in complex with Udp and Mn2+


Overview

The HNK-1 carbohydrate epitope is found on many neural cell adhesion molecules. Its structure is characterized by a terminal sulfated glucuronyl acid. The glucuronyltransferases, GlcAT-P and GlcAT-S, are involved in the biosynthesis of the HNK-1 epitope, GlcAT-P as the major enzyme. We overexpressed and purified the recombinant human GlcAT-P from Escherichia coli. Analysis of its enzymatic activity showed that it catalyzed the transfer reaction for N-acetyllactosamine (Galbeta1-4GlcNAc) but not lacto-N-biose (Galbeta1-3GlcNAc) as an acceptor substrate. Subsequently, we determined the first x-ray crystal structures of human GlcAT-P, in the absence and presence of a donor substrate product UDP, catalytic Mn(2+), and an acceptor substrate analogue N-acetyllactosamine (Galbeta1-4GlcNAc) or an asparagine-linked biantennary nonasaccharide. The asymmetric unit contains two independent molecules. Each molecule is an alpha/beta protein with two regions that constitute the donor and acceptor substrate binding sites. The UDP moiety of donor nucleotide sugar is recognized by conserved amino acid residues including a DXD motif (Asp(195)-Asp(196)-Asp(197)). Other conserved amino acid residues interact with the terminal galactose moiety of the acceptor substrate. In addition, Val(320) and Asn(321), which are located on the C-terminal long loop from a neighboring molecule, and Phe(245) contribute to the interaction with GlcNAc moiety. These three residues play a key role in establishing the acceptor substrate specificity.

About this Structure

1V83 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1., Kakuda S, Shiba T, Ishiguro M, Tagawa H, Oka S, Kajihara Y, Kawasaki T, Wakatsuki S, Kato R, J Biol Chem. 2004 May 21;279(21):22693-703. Epub 2004 Mar 1. PMID:14993226

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