1VRC

Complex of enzyme IIAmannose and the histidine-containing phosphocarrier protein HPr from escherichia coli nmr, restrained regularized mean structure

1VRC の概要

• エントリーDOI: 10.2210/pdb1vrc/pdb
• NMR情報: BMRB: 4264
• 分子名称: PTS system, mannose-specific IIAB component, Phosphocarrier protein HPr, PHOSPHITE ION (3 entities in total)
• 機能のキーワード: phosphotransferase, transferase, kinase, sugar transport, complex (transferase-phosphocarrier)
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: P69797 P0AA04
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 47928.25

構造登録者

Clore, G.M.,Williams, D.C. (登録日: 2005-02-21, 公開日: 2005-04-19, 最終更新日: 2023-12-27)

主引用文献

Williams, D.C.,Cai, M.,Suh, J.Y.,Peterkofsky, A.,Clore, G.M.
Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase system.
J.Biol.Chem., 280:20775-20784, 2005

PubMed Abstract: The solution structure of the 48-kDa IIA(Man)-HPr complex of the mannose branch of the Escherichia coli phosphotransferase system has been solved by NMR using conjoined rigid body/torsion angle-simulated annealing on the basis of intermolecular nuclear Overhauser enhancement data and residual dipolar couplings. IIA(Man) is dimeric and has two symmetrically related binding sites per dimer for HPr. A convex surface on HPr, formed primarily by helices 1 and 2, interacts with a deep groove at the interface of the two subunits of IIA(Man). The interaction surface on IIA(Man) is predominantly helical, comprising helix 3 from the subunit that bears the active site His-10 and helices 1, 4, and 5 from the other subunit. The total buried accessible surface area at the protein-protein interface is 1450 A(2). The binding sites on the two proteins are complementary in terms of shape and distribution of hydrophobic, hydrophilic, and charged residues. The active site histidines, His-10 of IIA(Man) and His-15 (italics indicate HPr residues) of HPr, are in close proximity. An associative transition state involving a pentacoordinate phosphoryl group with trigonal bipyramidal geometry bonded to the N-epsilon2 atom of His-10 and the N-delta1 atom of His-15 can be readily formed with negligible displacement in the backbone coordinates of the residues immediately adjacent to the active site histidines. Comparing the structures of complexes of HPr with three other structurally unrelated phosphotransferase system proteins, enzymes I, IIA(glucose), and IIA(mannitol), reveals a number of common features that provide a molecular basis for understanding how HPr specifically recognizes a wide range of diverse proteins.

PubMed: 15788390
DOI: 10.1074/jbc.M501986200

実験手法

SOLUTION NMR