1dg1

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[[Image:1dg1.gif|left|200px]]
[[Image:1dg1.gif|left|200px]]
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{{Structure
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|PDB= 1dg1 |SIZE=350|CAPTION= <scene name='initialview01'>1dg1</scene>, resolution 2.50&Aring;
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The line below this paragraph, containing "STRUCTURE_1dg1", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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{{STRUCTURE_1dg1| PDB=1dg1 | SCENE= }}
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|RELATEDENTRY=[[1aip|1AIP]], [[1b23|1B23]], [[1d2e|1D2E]], [[1dar|1DAR]], [[1efc|1EFC]], [[1efm|1EFM]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dg1 OCA], [http://www.ebi.ac.uk/pdbsum/1dg1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dg1 RCSB]</span>
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'''WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).'''
'''WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).'''
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[[Category: Jurnak, F.]]
[[Category: Jurnak, F.]]
[[Category: Yoder, M.]]
[[Category: Yoder, M.]]
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[[Category: alpha beta shift]]
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[[Category: Alpha beta shift]]
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[[Category: elongation factor]]
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[[Category: Elongation factor]]
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[[Category: gdp binding]]
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[[Category: Gdp binding]]
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[[Category: gtpase]]
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[[Category: Gtpase]]
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[[Category: trna binding]]
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[[Category: Trna binding]]
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[[Category: ts binding protein]]
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[[Category: Ts binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:48:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:40:58 2008''
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Revision as of 10:48, 2 May 2008

Image:1dg1.gif

Template:STRUCTURE 1dg1

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. 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 Page seeded by OCA on Fri May 2 13:48:57 2008

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