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1TEX

Mycobacterium smegmatis Stf0 Sulfotransferase with Trehalose

1TEX の概要
エントリーDOI10.2210/pdb1tex/pdb
関連するBIRD辞書のPRD_IDPRD_900006
分子名称Stf0 Sulfotransferase, alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose (3 entities in total)
機能のキーワードmycobacterium, sulfotransferase, sulfolipid, sulfation, trehalose, trehalose-2-sulfate, transferase
由来する生物種Mycobacterium smegmatis
タンパク質・核酸の鎖数4
化学式量合計131359.22
構造登録者
主引用文献Mougous, J.D.,Petzold, C.J.,Senaratne, R.H.,Lee, D.H.,Akey, D.L.,Lin, F.L.,Munchel, S.E.,Pratt, M.R.,Riley, L.W.,Leary, J.A.,Berger, J.M.,Bertozzi, C.R.
Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis.
Nat.Struct.Mol.Biol., 11:721-729, 2004
Cited by
PubMed Abstract: Sulfolipid-1 (SL-1) is an abundant sulfated glycolipid and potential virulence factor found in Mycobacterium tuberculosis. SL-1 consists of a trehalose-2-sulfate (T2S) disaccharide elaborated with four lipids. We identified and characterized a conserved mycobacterial sulfotransferase, Stf0, which generates the T2S moiety of SL-1. Biochemical studies demonstrated that the enzyme requires unmodified trehalose as substrate and is sensitive to small structural perturbations of the disaccharide. Disruption of stf0 in Mycobacterium smegmatis and M. tuberculosis resulted in the loss of T2S and SL-1 formation, respectively. The structure of Stf0 at a resolution of 2.6 A reveals the molecular basis of trehalose recognition and a unique dimer configuration that encloses the substrate into a bipartite active site. These data provide strong evidence that Stf0 carries out the first committed step in the biosynthesis of SL-1 and establish a system for probing the role of SL-1 in M. tuberculosis infection.
PubMed: 15258569
DOI: 10.1038/nsmb802
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.6 Å)
構造検証レポート
Validation report summary of 1tex
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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