1etu

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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1etu ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1etu ConSurf].
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== Publication Abstract from PubMed ==
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Structural details of the guanosine diphosphate binding to a modified form of elongation factor Tu from Escherichia coli, resulting from X-ray crystallographic studies, are reported. The protein elements that take part in the nucleotide binding are located in four loops connecting beta-strands with alpha-helices. These loops correspond to regions in primary sequences which show a high degree of homology when compared with other prokaryotic and eukaryotic elongation factors and initiation factor 2.
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Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography.,la Cour TF, Nyborg J, Thirup S, Clark BF EMBO J. 1985 Sep;4(9):2385-8. PMID:3908095<ref>PMID:3908095</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1etu" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 05:28, 5 June 2024

STRUCTURAL DETAILS OF THE BINDING OF GUANOSINE DIPHOSPHATE TO ELONGATION FACTOR TU FROM E. COLI AS STUDIED BY X-RAY CRYSTALLOGRAPHY

PDB ID 1etu

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