1etu

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[[Image:1etu.gif|left|200px]]
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{{STRUCTURE_1etu| PDB=1etu | SCENE= }}
{{STRUCTURE_1etu| PDB=1etu | SCENE= }}
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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'''
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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===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 3908095 is the PubMed ID number.
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{{ABSTRACT_PUBMED_3908095}}
==About this Structure==
==About this Structure==
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[[Category: Thirup, S.]]
[[Category: Thirup, S.]]
[[Category: Transport and protection protein]]
[[Category: Transport and protection protein]]
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Revision as of 22:58, 30 June 2008

Image:1etu.png

Template:STRUCTURE 1etu

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

Template:ABSTRACT PUBMED 3908095

About this Structure

1ETU is a Single protein structure. Full crystallographic information is available from OCA.

Reference

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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