Crystallization (Comment) | Organism |
---|---|
binary complex of UDP and ppGalNAcT-2 in crystal structure PDB: 2FFV | Homo sapiens |
dynamics of loop A dependent on presence of ligand and state of loop B | Homo sapiens |
dynamics of loop B reduced upon UDP-GalNAc (donor) binding but not further reduced by subsequent peptide (acceptor) binding | Homo sapiens |
flexibility of terminal residues of EA2 peptide in EA2-enzyme complex is reduced upon presence of a GalNAc moiety | Homo sapiens |
in presence of UDP or UDP and peptide no water molecule-dependent, large conformational changes | Homo sapiens |
low flexibility of EA2 peptide centre in EA2-enzyme complex | Homo sapiens |
PDB: 2FFU incl. substrates versus PDB: 2FFU lacking substrates: flexibility of catalytic and lectin domain independent of each others presence or distance | Homo sapiens |
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 |
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 |
single-displacement transfer mechanism revealed by simulations on crystal structure PDB: 2FFU | Homo sapiens |
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 | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | hydrated by a single water molecule in the presence of UDP-GalNAc or UDP-GalNAc and peptide | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q10471 | ppGalNAcT-2 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | ? | |
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 | Comment | Organism |
---|---|---|
ppGalNAcT | - |
Homo sapiens |
UDP-GalNAc polypeptides:N-acetyl-alpha-galactosaminyltransferase | - |
Homo sapiens |
UDP-N-acetylgalactosamine:polypeptide N-acetyl-alpha-galactosaminyltransferase | - |
Homo sapiens |
UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase | - |
Homo sapiens |