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2VK2

Crystal structure of a galactofuranose binding protein

2VK2 の概要
エントリーDOI10.2210/pdb2vk2/pdb
分子名称ABC TRANSPORTER PERIPLASMIC-BINDING PROTEIN YTFQ, beta-D-galactofuranose (3 entities in total)
機能のキーワードtransport protein, abc transport, galactofuranose, transport, periplasm
由来する生物種ESCHERICHIA COLI
タンパク質・核酸の鎖数1
化学式量合計33556.29
構造登録者
Muller, A.,Horler, R.S.P.,Thomas, G.H.,Wilson, K.S. (登録日: 2007-12-16, 公開日: 2009-05-19, 最終更新日: 2024-11-20)
主引用文献Horler, R.S.P.,Muller, A.,Williamson, D.C.,Potts, J.R.,Wilson, K.S.,Thomas, G.H.
Furanose-Specific Sugar Transport: Characterization of a Bacterial Galactofuranose-Binding Protein.
J.Biol.Chem., 284:31156-, 2009
Cited by
PubMed Abstract: The widespread utilization of sugars by microbes is reflected in the diversity and multiplicity of cellular transporters used to acquire these compounds from the environment. The model bacterium Escherichia coli has numerous transporters that allow it to take up hexoses and pentoses, which recognize the more abundant pyranose forms of these sugars. Here we report the biochemical and structural characterization of a transporter protein YtfQ from E. coli that forms part of an uncharacterized ABC transporter system. Remarkably the crystal structure of this protein, solved to 1.2 A using x-ray crystallography, revealed that YtfQ binds a single molecule of galactofuranose in its ligand binding pocket. Selective binding of galactofuranose over galactopyranose was also observed using NMR methods that determined the form of the sugar released from the protein. The pattern of expression of the ytfQRTyjfF operon encoding this transporter mirrors that of the high affinity galactopyranose transporter of E. coli, suggesting that this bacterium has evolved complementary transporters that enable it to use all the available galactose present during carbon limiting conditions.
PubMed: 19744923
DOI: 10.1074/JBC.M109.054296
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.2 Å)
構造検証レポート
Validation report summary of 2vk2
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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