From Proteopedia
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| - | [[Image:1dg1.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1dg1.png|left|200px]] |
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| | {{STRUCTURE_1dg1| PDB=1dg1 | SCENE= }} | | {{STRUCTURE_1dg1| PDB=1dg1 | SCENE= }} |
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| - | '''WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).'''
| + | ===WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8939740}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8939740 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8939740}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Trna binding]] | | [[Category: Trna binding]] |
| | [[Category: Ts binding protein]] | | [[Category: Ts binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:48:57 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:01:36 2008'' |
Revision as of 20:01, 30 June 2008
Template:STRUCTURE 1dg1
WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).
Template:ABSTRACT PUBMED 8939740
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 Mon Jun 30 23:01:36 2008
