1dg1
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(New page: 200px<br /><applet load="1dg1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dg1, resolution 2.50Å" /> '''WHOLE, UNMODIFIED, E...)
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Revision as of 11:08, 20 November 2007
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WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).
Overview
BACKGROUND: The bacterial elongation factor EF-Tu recognizes and, transports aminoacyl-tRNAs to mRNA-programmed ribosomes. EF-Tu shares many, structural and functional properties with other GTPases whose, conformations are regulated by guanine nucleotides. RESULTS: An intact, form of Escherichia coli EF-Tu complexed with GDP has been crystallized in, the presence of the EF-Tu-specific antibiotic GE2270 A. The, three-dimensional structure has been solved by X-ray diffraction analysis, and refined to a final crystallographic R factor of 17.2% at a resolution, of 2.5 A. The location of the GE2270 A antibiotic-binding site could not, be identified. CONCLUSIONS: The structure of EF-Tu-GDP is nearly identical, to that of a trypsin-modified form of EF-Tu-GDP, demonstrating, conclusively that the protease treatment had not altered any essential, structural features. The present structure represents the first view of an, ordered Switch I region in EF-Tu-GDP and reveals similarities with two, other GTPases complexed with GDP: Ran and ADP-ribosylation factor-1. A, comparison of the Switch I regions of the GTP and GDP forms of EF-Tu also, reveals that a segment, six amino acids in length, completely converts, from an alpha helix in the GTP complex to beta secondary structure in the, GDP form. The alpha to beta switch in EF-Tu may represent a prototypical, activation mechanism for other protein families.
About this Structure
1DG1 is a Single protein structure of sequence from Escherichia coli with MG and GDP as ligands. Full crystallographic information is available from OCA.
Reference
An alpha to beta conformational switch in EF-Tu., Abel K, Yoder MD, Hilgenfeld R, Jurnak F, Structure. 1996 Oct 15;4(10):1153-9. PMID:8939740
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