1F3G

THREE-DIMENSIONAL STRUCTURE OF THE ESCHERICHIA COLI PHOSPHOCARRIER PROTEIN III GLC

Summary for 1F3G

• Entry DOI: 10.2210/pdb1f3g/pdb
• Descriptor: GLUCOSE-SPECIFIC PHOSPHOCARRIER PROTEIN IIAGLC (2 entities in total)
• Functional Keywords: phosphotransferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P69783
• Total number of polymer chains: 1
• Total formula weight: 17337.84

Authors

Worthylake, D.,Meadow, N.,Roseman, S.,Liao, D.-I.,Herzberg, O.,Remington, S.J. (deposition date: 1991-08-28, release date: 1993-10-31, Last modification date: 2024-02-07)

Primary citation

Worthylake, D.,Meadow, N.D.,Roseman, S.,Liao, D.I.,Herzberg, O.,Remington, S.J.
Three-dimensional structure of the Escherichia coli phosphocarrier protein IIIglc.
Proc.Natl.Acad.Sci.USA, 88:10382-10386, 1991

PubMed Abstract: The crystal structure of a proteolytically modified form of the Escherichia coli phosphocarrier and signal transducing protein IIIglc has been determined by multiple isomorphous and molecular replacement. The model has been refined to an R-factor of 0.166 for data between 6- and 2.1-A resolution with an rms deviation of 0.020 A from ideal bond lengths and 3.2 degrees from ideal bond angles. The molecule is a beta-sheet sandwich, with six antiparallel strands on either side. Several short distorted helices line the periphery of the active site, which is a shallow extremely hydrophobic depression approximately 18 A in diameter near the center of one face. The side chains of the active site histidine residues 75 and 90 face each other at the center of the depression, with the N3 positions exposed to solvent, separated by 3.3 A in an excellent position to form adducts with phosphate. Chloroplatinate forms a divalent adduct with both histidyl side chains, suggesting that the phosphodonor reaction might proceed through a similar transition state. The hydrophobic patch forms the primary crystal contact, suggesting a mode of association of IIIglc with other components of the phosphoenolpyruvate-dependent phosphotransferase system.

PubMed: 1961703
DOI: 10.1073/pnas.88.23.10382

Experimental method

X-RAY DIFFRACTION (2.1 Å)