1v83
From Proteopedia
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|PDB= 1v83 |SIZE=350|CAPTION= <scene name='initialview01'>1v83</scene>, resolution 1.9Å | |PDB= 1v83 |SIZE=350|CAPTION= <scene name='initialview01'>1v83</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene> | + | |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'-DIPHOSPHATE'>UDP</scene> |
- | |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] | + | |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= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1v82|1V82]], [[1v84|1V84]] | ||
+ | |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.]] | ||
- | [[Category: MN]] | ||
- | [[Category: TLA]] | ||
- | [[Category: UDP]] | ||
[[Category: glycocyltransferase]] | [[Category: glycocyltransferase]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''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
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, resolution 1.9Å | |||||||
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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
Page seeded by OCA on Mon Mar 31 00:20:42 2008