1VRC

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

Summary for 1VRC

• Entry DOI: 10.2210/pdb1vrc/pdb
• NMR Information: BMRB: 4264
• Descriptor: PTS system, mannose-specific IIAB component, Phosphocarrier protein HPr, PHOSPHITE ION (3 entities in total)
• Functional Keywords: phosphotransferase, transferase, kinase, sugar transport, complex (transferase-phosphocarrier)
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P69797 P0AA04
• Total number of polymer chains: 4
• Total formula weight: 47928.25

Authors

Clore, G.M.,Williams, D.C. (deposition date: 2005-02-21, release date: 2005-04-19, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

SOLUTION NMR