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4N3B

Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1 pro-repeat2(1-26)E10Q and UDP-5SGlcNAc

4N3B の概要
エントリーDOI10.2210/pdb4n3b/pdb
関連するPDBエントリー4N39 4N3A 4N3C
分子名称UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit, Host cell factor 1, (2S,3R,4R,5S,6R)-3-(acetylamino)-4,5-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-thiopyran-2-yl [(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate, ... (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84291.80
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.17 Å)
構造検証レポート
Validation report summary of 4n3b
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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