1f3g
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1f3g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f3g, resolution 2.1Å" /> '''THREE-DIMENSIONAL STR...)
Next diff →
Revision as of 12:27, 20 November 2007
|
THREE-DIMENSIONAL STRUCTURE OF THE ESCHERICHIA COLI PHOSPHOCARRIER PROTEIN III GLC
Overview
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.
About this Structure
1F3G is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the Escherichia coli phosphocarrier protein IIIglc., Worthylake D, Meadow ND, Roseman S, Liao DI, Herzberg O, Remington SJ, Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10382-6. PMID:1961703
Page seeded by OCA on Tue Nov 20 14:34:48 2007
