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2d7i

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[[Image:2d7i.jpg|left|200px]]<br /><applet load="2d7i" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2d7i.jpg|left|200px]]
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caption="2d7i, resolution 2.5&Aring;" />
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'''Crsytal structure of pp-GalNAc-T10 with UDP, GalNAc and Mn2+'''<br />
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{{Structure
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|PDB= 2d7i |SIZE=350|CAPTION= <scene name='initialview01'>2d7i</scene>, resolution 2.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=UDP:URIDINE-5'-DIPHOSPHATE'>UDP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Polypeptide_N-acetylgalactosaminyltransferase Polypeptide N-acetylgalactosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.41 2.4.1.41]
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|GENE=
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}}
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'''Crsytal structure of pp-GalNAc-T10 with UDP, GalNAc and Mn2+'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2D7I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=NGA:'>NGA</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=UDP:'>UDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Polypeptide_N-acetylgalactosaminyltransferase Polypeptide N-acetylgalactosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.41 2.4.1.41] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D7I OCA].
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2D7I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D7I OCA].
==Reference==
==Reference==
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Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)., Kubota T, Shiba T, Sugioka S, Furukawa S, Sawaki H, Kato R, Wakatsuki S, Narimatsu H, J Mol Biol. 2006 Jun 9;359(3):708-27. Epub 2006 Apr 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16650853 16650853]
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Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)., Kubota T, Shiba T, Sugioka S, Furukawa S, Sawaki H, Kato R, Wakatsuki S, Narimatsu H, J Mol Biol. 2006 Jun 9;359(3):708-27. Epub 2006 Apr 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16650853 16650853]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Polypeptide N-acetylgalactosaminyltransferase]]
[[Category: Polypeptide N-acetylgalactosaminyltransferase]]
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[[Category: rossmann fold]]
[[Category: rossmann fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:23:57 2008''

Revision as of 14:23, 20 March 2008


PDB ID 2d7i

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands: , , and
Activity: Polypeptide N-acetylgalactosaminyltransferase, with EC number 2.4.1.41
Coordinates: save as pdb, mmCIF, xml



Crsytal structure of pp-GalNAc-T10 with UDP, GalNAc and Mn2+


Overview

Mucin-type O-glycans are important carbohydrate chains involved in differentiation and malignant transformation. Biosynthesis of the O-glycan is initiated by the transfer of N-acetylgalactosamine (GalNAc) which is catalyzed by UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-Ts). Here we present crystal structures of the pp-GalNAc-T10 isozyme, which has specificity for glycosylated peptides, in complex with the hydrolyzed donor substrate UDP-GalNAc and in complex with GalNAc-serine. A structural comparison with uncomplexed pp-GalNAc-T1 suggests that substantial conformational changes occur in two loops near the catalytic center upon donor substrate binding, and that a distinct interdomain arrangement between the catalytic and lectin domains forms a narrow cleft for acceptor substrates. The distance between the catalytic center and the carbohydrate-binding site on the lectin beta sub-domain influences the position of GalNAc glycosylation on GalNAc-glycosylated peptide substrates. A chimeric enzyme in which the two domains of pp-GalNAc-T10 are connected by a linker from pp-GalNAc-T1 acquires activity toward non-glycosylated acceptors, identifying a potential mechanism for generating the various acceptor specificities in different isozymes to produce a wide range of O-glycans.

About this Structure

2D7I is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)., Kubota T, Shiba T, Sugioka S, Furukawa S, Sawaki H, Kato R, Wakatsuki S, Narimatsu H, J Mol Biol. 2006 Jun 9;359(3):708-27. Epub 2006 Apr 19. PMID:16650853

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