4N3C

Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1 pro-repeat2(1-26) and UDP-GlcNAc

4N3C の概要

• エントリーDOI: 10.2210/pdb4n3c/pdb
• 関連するPDBエントリー: 4N39 4N3A 4N3B
• 分子名称: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit, Host cell factor 1, URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE, ... (4 entities in total)
• 機能のキーワード: glycosyltransferase, o-glcnac transferase, proteolysis substrate, tpr domain, tpr binding, transferase-substrate complex, transferase/substrate
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Isoform 2: Mitochondrion. Isoform 3: Cytoplasm. Isoform 4: Cytoplasm: O15294; Cytoplasm: P51610
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84276.72

構造登録者

Lazarus, M.B.,Herr, W.,Walker, S. (登録日: 2013-10-06, 公開日: 2014-01-01, 最終更新日: 2024-02-28)

主引用文献

Lazarus, M.B.,Jiang, J.,Kapuria, V.,Bhuiyan, T.,Janetzko, J.,Zandberg, W.F.,Vocadlo, D.J.,Herr, W.,Walker, S.
HCF-1 is cleaved in the active site of O-GlcNAc transferase.
Science, 342:1235-1239, 2013

PubMed Abstract: Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT). We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc. The conformation is similar to that of a glycosylation-competent peptide substrate. Cleavage occurs between cysteine and glutamate residues and results in a pyroglutamate product. Conversion of the cleavage site glutamate into serine converts an HCF-1 proteolytic repeat into a glycosylation substrate. Thus, protein glycosylation and HCF-1 cleavage occur in the same active site.

PubMed: 24311690
DOI: 10.1126/science.1243990

実験手法

X-RAY DIFFRACTION (2.55 Å)