X‐ray determination of the GDP‐binding site of <i>Escherichia coli</i> elongation factor Tu by substitution with ppGpp

Suck, Dietrich; Kabsch, Wolfgang

doi:10.1016/0014-5793(81)81048-4

Cited by 15 publications

(1 citation statement)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2). This agrees with our observations for elongation factor Tu GDP at 6-A resolution (21) in which the highest density turned out to be the bound nucleotide (22).…”

Section: Mgatpsupporting

confidence: 83%

Three-dimensional structure of the complex of skeletal muscle actin and bovine pancreatic DNAse I at 6-A resolution.

Suck¹,

Kabsch²,

Mannherz³

1981

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The structure ofrabbit skeletal muscle actin complexed with bovine pancreatic DNase I has been determined by x-ray crystallographic methods at 6-A resolution. The analysis was based on a new orthorhombic crystal form, space group P212121, with one complex in the asymmetric unit. Six isomorphous heavyatom derivatives yielding an overall figure of merit of 0.72 have been used to calculate the electron-density map. Molecular models for actin and DNase I' derived from this map have dimensions 67 X 40 X 37 A and 50 X 50 X 40 A, respectively. The actin molecule is elongated and consists of a larger and a smaller domain, each containing density regions resembling a central 3-pleated sheet surrounded by a-helices. The highest electron-density peak is found in the cleft between the two domains, perhaps indicating the bound ATP. Observed crystal contacts between actin molecules and a model for the F-actin filament are discussed. Two high-affinity Ca2-binding sites which also bind Ba2+ have been located at the surface of the DNase I molecule.

show abstract

“…2). This agrees with our observations for elongation factor Tu GDP at 6-A resolution (21) in which the highest density turned out to be the bound nucleotide (22).…”

Section: Mgatpsupporting

confidence: 83%

Three-dimensional structure of the complex of skeletal muscle actin and bovine pancreatic DNAse I at 6-A resolution.

Suck¹,

Kabsch²,

Mannherz³

1981

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

Specific alterations of the EF-Tu polypeptide chain considered in the light of its three-dimensional structure.

Duisterwinkel¹,

Kraal²,

Graaf³

et al. 1984

The EMBO Journal

View full text Add to dashboard Cite

Specific alterations of the elongation factor Tu (EF‐Tu) polypeptide chain have been identified in a number of mutant species of this elongation factor. In two species, Ala‐375, located on domain II, was found by amino acid analysis to be replaced by Thr and Val, respectively. These replacements substantially lower the affinity of EF‐Tu.GDP for the antibiotic kirromycin. Since kirromycin can be cross‐linked to Lys‐357, also located on domain II but structurally very far from Ala‐375, these data suggest that the replacements alter the relative position of domains I and II. The Ala‐375 replacements also lower the dissociation rates of the binary complexes EF‐Tu.GTP and the binding constants for EF‐Tu.GTP and Phe‐tRNA. It is conceivable that these effects are also mediated by movements of domains I and II relative to each other. Replacement of Gly‐222 by Asp has been found in another mutant by DNA sequence analysis of the cloned tufB gene, coding for this mutant EF‐Tu. Gly‐222 is part of a structural domain, characteristic for a variety of nucleotide binding enzymes. Its replacement by Asp does not abolish the ability of EF‐Tu to sustain protein synthesis. It increases the dissociation rate of EF‐Tu.GTP by approximately 30%. In the presence of kirromycin this mutant species of EF‐Tu.GDP does not bind to the ribosome, in contrast to its wild‐type counterpart. A possible explanation is now open for experimental verification.

show abstract

Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography.

Cour¹,

Nyborg²,

Thirup³

et al. 1985

The EMBO Journal

397

171

View full text Add to dashboard Cite

Structural details of the guanosine diphosphate binding to a modified form of elongation factor Tu from Escherchia coli, resulting from X-ray crystallographic studies, are reported. The protein elements that take part in the nucleotide binding are located in four loops connecting (B-strands with ct-helices.These loops correspond to regions in primary sequences which show a high degree of homology when compared with other prokaryotic and eukaryotic elongation factors and initiation factor 2.

show abstract

X‐ray determination of the GDP‐binding site of Escherichia coli elongation factor Tu by substitution with ppGpp

Cited by 15 publications

References 12 publications

Three-dimensional structure of the complex of skeletal muscle actin and bovine pancreatic DNAse I at 6-A resolution.

Three-dimensional structure of the complex of skeletal muscle actin and bovine pancreatic DNAse I at 6-A resolution.

Specific alterations of the EF-Tu polypeptide chain considered in the light of its three-dimensional structure.

Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography.

Contact Info

Product

Resources

About