2hcj

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Revision as of 09:33, 21 November 2007

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spinqualitylabelsall models 2hcj, resolution 2.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

"Trypsin-modified Elongation Factor Tu in complex with tetracycline"

Overview

Two crystal forms of a complex between trypsin-modified elongation factor, Tu-MgGDP from Escherichia coli and the antibiotic tetracycline have been, solved by X-ray diffraction analysis to resolutions of 2.8 and 2.1 A, respectively. In the P2(1) form, cocrystals were grown from a solution, mixture of the protein and tetracycline. Six copies of the, trypsin-modified EF-Tu-MgGDP-tetracycline complex are arranged as three, sets of dimers in the asymmetric unit. In the second crystal form, tetracycline was diffused into P4(3)2(1)2 crystals, resulting in a, monomeric complex in the asymmetric unit. Atomic coordinates have been, refined to crystallographic R factors of 18.0% for the P2(1) form and, 20.0% for the P4(3)2(1)2 form. In both complexes, tetracycline makes, significant interactions with the GTPase active site of EF-Tu. The, phenoldiketone moiety of tetracycline interacts directly with the Mg(2+), the alpha-phosphate group of GDP and two amino acids, Thr25 and Asp80, which are conserved in the GX(4)GKS/T and DX(2)G sequence motifs found in, all GTPases and many ATPases. The molecular complementarity, previously, unrecognized between invariant groups present in all GTPase/ATPases and, the active moiety of tetracycline, may have wide-ranging implications for, all drugs containing the phenoldiketone moiety as well as for the design, of new compounds targeted against a broad range of GTPases or ATPases.

About this Structure

2HCJ is a Protein complex structure of sequences from Escherichia coli with MG, NA, SO4, TAC, GDP and GLV as ligands. Full crystallographic information is available from OCA.

Reference

Molecular complementarity between tetracycline and the GTPase active site of elongation factor Tu., Heffron SE, Mui S, Aorora A, Abel K, Bergmann E, Jurnak F, Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1392-400. Epub, 2006 Oct 18. PMID:17057344

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