4AYL

Molecular structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen

4AYL の概要

• エントリーDOI: 10.2210/pdb4ayl/pdb
• 関連するPDBエントリー: 4AYJ
• 分子名称: BOGT-METAL-INDEPENDENT GLYCOSYLTRANSFERASE, CALCIUM ION, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (5 entities in total)
• 機能のキーワード: transferase, histo-blood group enzyme
• 由来する生物種: BACTEROIDES OVATUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29351.89

構造登録者

Thiyagarajan, N.,Pham, T.T.K.,Stinsonb, B.,Sundriyala, A.,Tumbale, P.,Lizotte-Waniewskib, M.,Brewb, K.,Acharya, K.R. (登録日: 2012-06-21, 公開日: 2012-12-19, 最終更新日: 2023-12-20)

主引用文献

Thiyagarajan, N.,Pham, T.T.K.,Stinson, B.,Sundriyal, A.,Tumbale, P.,Lizotte-Waniewski, M.,Brew, K.,Acharya, K.R.
Structure of a Metal-Independent Bacterial Glycosyltransferase that Catalyzes the Synthesis of Histo-Blood Group a Antigen
Sci.Rep., 2:940-, 2012

PubMed Abstract: Histo-blood group antigens (HBGAs) are a source of antigenic variation between individuals that modulates resistance and susceptibility to pathogens and is a barrier to the spread of enveloped viruses. HBGAs are also produced by a few prokaryotes where they are synthesized by glycosyltransferases (GTs) related to human HBGA synthases. Here we report the first structure of a bacterial GT of this family, from an intestinal resident, Bacteroides ovatus. Unlike its mammalian homologues and other GTs with similar folds, this protein lacks a metal-binding Asp-X-Asp motif and is fully active in the absence of divalent metal ions, yet is strikingly similar in structure and in its interactions with substrates to structurally characterized mammalian metal-dependent mammalian homologues. This shows how an apparently major divergence in catalytic properties can be accommodated by minor structural adjustments and illustrates the structural underpinnings of horizontal transfer of a functional gene from prokaryotes to vertebrates.

PubMed: 23230506
DOI: 10.1038/SREP00940

実験手法

X-RAY DIFFRACTION (1.919 Å)