1VKR

STRUCTURE OF IIB DOMAIN OF THE MANNITOL-SPECIFIC PERMEASE ENZYME II

1VKR の概要

• エントリーDOI: 10.2210/pdb1vkr/pdb
• 分子名称: mannitol-specific PTS system enzyme IIABC components (1 entity in total)
• 機能のキーワード: phosphotransferase, transferase, kinase, sugar transport
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P00550
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13462.08

構造登録者

Clore, G.M.,Legler, P.M.,Cai, M. (登録日: 2004-06-14, 公開日: 2004-09-21, 最終更新日: 2023-12-27)

主引用文献

Legler, P.M.,Cai, M.,Peterkofsky, A.,Clore, G.M.
Three-dimensional Solution Structure of the Cytoplasmic B Domain of the Mannitol Transporter II-Mannitol of the Escherichia coli Phosphotransferase System.
J.Biol.Chem., 279:39115-39121, 2004

PubMed Abstract: The solution structure of the cytoplasmic B domain of the mannitol (Mtl) transporter (II(Mtl)) from the mannitol branch of the Escherichia coli phosphotransferase system has been solved by multidimensional NMR spectroscopy with extensive use of residual dipolar couplings. The ordered IIB(Mtl) domain (residues 375-471 of II(Mtl)) consists of a four-stranded parallel beta-sheet flanked by two helices (alpha(1) and alpha(3)) on one face and helix alpha(2) on the opposite face with a characteristic Rossmann fold comprising two right-handed beta(1)alpha(1)beta(2) and beta(3)alpha(2)beta(4) motifs. The active site loop is structurally very similar to that of the eukaryotic protein tyrosine phosphatases, with the active site cysteine (Cys-384) primed in the thiolate state (pK(a) < 5.6) for nucleophilic attack at the phosphorylated histidine (His-554) of the IIA(Mtl) domain through stabilization by hydrogen bonding interactions with neighboring backbone amide groups at positions i + 2/3/4 from Cys-384 and with the hydroxyl group of Ser-391 at position i + 7. Modeling of the phosphorylated state of IIB(Mtl) suggests that the phosphoryl group can be readily stabilized by hydrogen bonding interactions with backbone amides in the i + 2/4/5/6/7 positions as well as with the hydroxyl group of Ser390 at position i + 6. Despite the absence of any significant sequence identity, the structure of IIB(Mtl) is remarkably similar to the structures of bovine protein tyrosine phosphatase (which contains two long insertions relative to IIB(Mtl)) and the cytoplasmic B component of enzyme II(Chb), which fulfills an analogous role to IIB(Mtl) in the N,N'-diacetylchitobiose branch of the phosphotransferase system. All three proteins utilize a cysteine residue in the nucleophilic attack of a phosphoryl group covalently bound to another protein.

PubMed: 15258141
DOI: 10.1074/jbc.M406764200

実験手法

SOLUTION NMR