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Literature summary extracted from

  • Milac, A.L.; Buchete, N.V.; Fritz, T.A.; Hummer, G.; Tabak, L.A.
    Substrate-induced conformational changes and dynamics of UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase-2 (2007), J. Mol. Biol., 373, 439-451.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.41 binary complex of UDP and ppGalNAcT-2 in crystal structure PDB: 2FFV Homo sapiens
2.4.1.41 dynamics of loop A dependent on presence of ligand and state of loop B Homo sapiens
2.4.1.41 dynamics of loop B reduced upon UDP-GalNAc (donor) binding but not further reduced by subsequent peptide (acceptor) binding Homo sapiens
2.4.1.41 flexibility of terminal residues of EA2 peptide in EA2-enzyme complex is reduced upon presence of a GalNAc moiety Homo sapiens
2.4.1.41 in presence of UDP or UDP and peptide no water molecule-dependent, large conformational changes Homo sapiens
2.4.1.41 low flexibility of EA2 peptide centre in EA2-enzyme complex Homo sapiens
2.4.1.41 PDB: 2FFU incl. substrates versus PDB: 2FFU lacking substrates: flexibility of catalytic and lectin domain independent of each others presence or distance Homo sapiens
2.4.1.41 PDB: 2FFV versus PDB: 2FFU: large conformational changes (13 to 24 Å) in catalytic domain upon peptide binding and processing, loop A (AA89-98), loop B (AA361-377) Homo sapiens
2.4.1.41 PDB: 2FFV versus PDB: 2FFU: small conformational changes (4 to 5 Å) of protein backbone upon peptide binding and processing, loop C (AA127-134), loop D (AA287-297), loop E (AA330-333) Homo sapiens
2.4.1.41 single-displacement transfer mechanism revealed by simulations on crystal structure PDB: 2FFU Homo sapiens
2.4.1.41 water molecule-dependent rotation of W331 side chain (WGGEN motif within loop E) that triggers loop B opening in the absence of substrate UDP-GalNAc and facilitates donor access into the active site as well as product release Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.41 Mn2+ hydrated by a single water molecule in the presence of UDP-GalNAc or UDP-GalNAc and peptide Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide Homo sapiens mucin-type O-linked glycosylation of serine or threonine residues UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.41 Homo sapiens Q10471 ppGalNAcT-2
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.41 UDP-GalNAc + EA2 ternary complex of ppGalNAcT-2 in crystal structure PDB: 2FFU, UDP-GalNAc binding results in the closed confirmation of loop B which stabilises loop A by binding of loop A (N102) to loop B (R362), EA2 peptide binds in an extended confirmation Homo sapiens GalNAc-EA2 + UDP binary complex of UDP and ppGalNAcT-2 in crystal structure PDB: 2FFV ?
2.4.1.41 UDP-N-acetyl-D-galactosamine + polypeptide mucin-type O-linked glycosylation of serine or threonine residues Homo sapiens UDP + N-acetyl-D-galactosaminyl-polypeptide
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.41 ppGalNAcT
-
 Homo sapiens
2.4.1.41 UDP-GalNAc polypeptides:N-acetyl-alpha-galactosaminyltransferase
-
 Homo sapiens
2.4.1.41 UDP-N-acetylgalactosamine:polypeptide N-acetyl-alpha-galactosaminyltransferase
-
 Homo sapiens
2.4.1.41 UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase
-
 Homo sapiens