4PQG
Crystal structure of the pneumococcal O-GlcNAc transferase GtfA in complex with UDP and GlcNAc
4PQG の概要
| エントリーDOI | 10.2210/pdb4pqg/pdb |
| 分子名称 | Glycosyltransferase Gtf1, URIDINE-5'-DIPHOSPHATE, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| 機能のキーワード | o-glcnac transferase, gt-b fold, rossmann fold, gtfb, transferase |
| 由来する生物種 | Streptococcus pneumoniae |
| 細胞内の位置 | Cytoplasm: Q97P84 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 118970.18 |
| 構造登録者 | Shi, W.W.,Jiang, Y.L.,Zhu, F.,Yang, Y.H.,Wu, H.,Ren, Y.M.,Chen, Y.,Zhou, C.Z. (登録日: 2014-03-03, 公開日: 2014-06-18, 最終更新日: 2024-02-28) |
| 主引用文献 | Shi, W.W.,Jiang, Y.L.,Zhu, F.,Yang, Y.H.,Shao, Q.Y.,Yang, H.B.,Ren, Y.M.,Wu, H.,Chen, Y.,Zhou, C.Z. Structure of a Novel O-Linked N-Acetyl-d-glucosamine (O-GlcNAc) Transferase, GtfA, Reveals Insights into the Glycosylation of Pneumococcal Serine-rich Repeat Adhesins. J.Biol.Chem., 289:20898-20907, 2014 Cited by PubMed Abstract: Protein glycosylation catalyzed by the O-GlcNAc transferase (OGT) plays a critical role in various biological processes. In Streptococcus pneumoniae, the core enzyme GtfA and co-activator GtfB form an OGT complex to glycosylate the serine-rich repeat (SRR) of adhesin PsrP (pneumococcal serine-rich repeat protein), which is involved in the infection and pathogenesis. Here we report the 2.0 Å crystal structure of GtfA, revealing a β-meander add-on domain beyond the catalytic domain. It represents a novel add-on domain, which is distinct from the all-α-tetratricopeptide repeats in the only two structure-known OGTs. Structural analyses combined with binding assays indicate that this add-on domain contributes to forming an active GtfA-GtfB complex and recognizing the acceptor protein. In addition, the in vitro glycosylation system enables us to map the O-linkages to the serine residues within the first SRR of PsrP. These findings suggest that fusion with an add-on domain might be a universal mechanism for diverse OGTs that recognize varying acceptor proteins/peptides. PubMed: 24936067DOI: 10.1074/jbc.M114.581934 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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