Structural constraints on the complex of elongation factor Tu with magnesium guanosine diphosphate from rotational-echo double-resonance NMR

✍ Scribed by Lynda M McDowell; Diane Barkan; G.Edwin Wilson; Jacob Schaefer

• Book ID: 104357818
• Publisher: Elsevier Science
• Year: 1996
• Tongue: English
• Weight: 672 KB
• Volume: 7
• Category: Article
• ISSN: 0926-2040
• DOI: 10.1016/s0926-2040(96)01270-2

✦ Synopsis

Rotational-echo, double-resonance (REDOR) NMR measurements of 3'P-'5N dipolar couplings have been made on a complex of Mg guanosine diphosphate (MgGDP) with uniformly "N-labeled elongation factor Tu. The complex was embedded in a lyophilized buffer glass. The observed 15N REDOR dephasing by 31 P was accounted for quantitatively by distances from "N of Gly23 and Lys24 to P, and Pp of MgGDP as determined by X-ray crystallography of a MgGDP complex formed using an elongation factor Tu that is missing a 15 residue loop in the vicinity of the binding site.