1dg1
From Proteopedia
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|PDB= 1dg1 |SIZE=350|CAPTION= <scene name='initialview01'>1dg1</scene>, resolution 2.50Å | |PDB= 1dg1 |SIZE=350|CAPTION= <scene name='initialview01'>1dg1</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1aip|1AIP]], [[1b23|1B23]], [[1d2e|1D2E]], [[1dar|1DAR]], [[1efc|1EFC]], [[1efm|1EFM]] | ||
| + | |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> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Jurnak, F.]] | [[Category: Jurnak, F.]] | ||
[[Category: Yoder, M.]] | [[Category: Yoder, M.]] | ||
| - | [[Category: GDP]] | ||
| - | [[Category: MG]] | ||
[[Category: alpha beta shift]] | [[Category: alpha beta shift]] | ||
[[Category: elongation factor]] | [[Category: elongation factor]] | ||
| Line 35: | Line 36: | ||
[[Category: ts binding protein]] | [[Category: ts binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:40:58 2008'' |
Revision as of 16:41, 30 March 2008
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1AIP, 1B23, 1D2E, 1DAR, 1EFC, 1EFM
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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