Structural constraints on the complex of elongation factor Tu with magnesium guanosine diphosphate from rotational-echo double-resonance NMR.
Rotational-echo, double-resonance (REDOR) NMR measurements of 31P-15N dipolar couplings have been made on a complex of Mg guanosine diphosphate (MgGDP) with uniformly 15N-labeled elongation factor Tu. The complex was embedded in a lyophilized buffer glass. The observed 15N REDOR dephasing by 31P was accounted for quantitatively by distances from 15N of Gly23 and Lys24 to P alpha and P beta of MgGDP as determined by X-ray crystallography of MgGDP complex formed using an elongation factor Tu that is missing a 15 residue loop in the vicinity of the binding site.
McDowell
L M
LM
Department of Chemistry, Washington University, St. Louis, MO 63130, USA.
Barkan
D
D
Wilson
G E
GE
Schaefer
J
J
D001665:Binding Sites; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D006153:Guanosine Diphosphate / Q000737:chemistry* / Q000378:metabolism; D008274:Magnesium / Q000737:chemistry / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation
D006153:Guanosine Diphosphate; D010444:Peptide Elongation Factor Tu; D008274:Magnesium