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6Q4W

Structure of MPT-1, a GDP-Man-dependent mannosyltransferase from Leishmania mexicana

6Q4W の概要
エントリーDOI10.2210/pdb6q4w/pdb
分子名称LmxM MPT-1 (2 entities in total)
機能のキーワードtransferase
由来する生物種Leishmania mexicana (strain MHOM/GT/2001/U1103)
タンパク質・核酸の鎖数2
化学式量合計78010.16
構造登録者
主引用文献Sernee, M.F.,Ralton, J.E.,Nero, T.L.,Sobala, L.F.,Kloehn, J.,Vieira-Lara, M.A.,Cobbold, S.A.,Stanton, L.,Pires, D.E.V.,Hanssen, E.,Males, A.,Ward, T.,Bastidas, L.M.,van der Peet, P.L.,Parker, M.W.,Ascher, D.B.,Williams, S.J.,Davies, G.J.,McConville, M.J.
A Family of Dual-Activity Glycosyltransferase-Phosphorylases Mediates Mannogen Turnover and Virulence in Leishmania Parasites.
Cell Host Microbe, 26:385-399.e9, 2019
Cited by
PubMed Abstract: Parasitic protists belonging to the genus Leishmania synthesize the non-canonical carbohydrate reserve, mannogen, which is composed of β-1,2-mannan oligosaccharides. Here, we identify a class of dual-activity mannosyltransferase/phosphorylases (MTPs) that catalyze both the sugar nucleotide-dependent biosynthesis and phosphorolytic turnover of mannogen. Structural and phylogenic analysis shows that while the MTPs are structurally related to bacterial mannan phosphorylases, they constitute a distinct family of glycosyltransferases (GT108) that have likely been acquired by horizontal gene transfer from gram-positive bacteria. The seven MTPs catalyze the constitutive synthesis and turnover of mannogen. This metabolic rheostat protects obligate intracellular parasite stages from nutrient excess, and is essential for thermotolerance and parasite infectivity in the mammalian host. Our results suggest that the acquisition and expansion of the MTP family in Leishmania increased the metabolic flexibility of these protists and contributed to their capacity to colonize new host niches.
PubMed: 31513773
DOI: 10.1016/j.chom.2019.08.009
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.55 Å)
構造検証レポート
Validation report summary of 6q4w
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2024-10-30に公開中

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