1etu

From Proteopedia
Revision as of 15:11, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1etu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1etu, resolution 2.9Å" /> '''STRUCTURAL DETAILS OF...)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search
File:1etu.gif


1etu, resolution 2.9Å

Drag the structure with the mouse to rotate

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] with MG and GDP as ligands. 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

Page seeded by OCA on Tue Nov 20 14:18:42 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA