2D7I

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

2D7I の概要

• エントリーDOI: 10.2210/pdb2d7i/pdb
• 関連するPDBエントリー: 2D7R
• 分子名称: Polypeptide N-acetylgalactosaminyltransferase 10, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: beta trefoil, rossmann fold, transferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 67019.43

構造登録者

Kubota, T.,Shiba, T.,Sugioka, S.,Kato, R.,Wakatsuki, S.,Narimatsu, H. (登録日: 2005-11-21, 公開日: 2006-11-07, 最終更新日: 2024-10-16)

主引用文献

Kubota, T.,Shiba, T.,Sugioka, S.,Furukawa, S.,Sawaki, H.,Kato, R.,Wakatsuki, S.,Narimatsu, H.
Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)
J.Mol.Biol., 359:708-727, 2006

PubMed Abstract: 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.

PubMed: 16650853
DOI: 10.1016/j.jmb.2006.03.061

実験手法

X-RAY DIFFRACTION (2.5 Å)