1etu: Difference between revisions

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|PDB= 1etu |SIZE=350|CAPTION= <scene name='initialview01'>1etu</scene>, resolution 2.9&Aring;
|PDB= 1etu |SIZE=350|CAPTION= <scene name='initialview01'>1etu</scene>, resolution 2.9&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
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[[Category: transport and protection protein]]
[[Category: transport and protection protein]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:00:19 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:41:58 2008''

Revision as of 12:41, 23 March 2008

File:1etu.gif


PDB ID 1etu

Drag the structure with the mouse to rotate
, resolution 2.9Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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.

About this StructureAbout this Structure

1ETU is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

ReferenceReference

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

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