1. Volume 6, Issue 5, Pages 1261-1266 (November 2000)
Structural Basis for Nucleotide Exchange and Competition with tRNA in the Yeast Elongation Factor Complex eEF1A:eEF1Bα 
Gregers Rom Andersen, Lise Pedersen, Louis Valente, Ishita Chatterjee, Terri Goss Kinzy, Morten Kjeldgaard, Jens Nyborg 
Molecular Cell 
Volume 6, Issue 5, Pages (November 2000)
DOI: /S (00)

2. Figure 1 Structure Determination
(A) Electron density around Phe-163b from the experimental map contoured at 1.35 σ with the final refined model superimposed. A water molecule is marked “w”.
(B) Cartoon of the eEF1A:eEF1Bα complex. Domain 1 (magenta) of eEF1A contains the binding site for the nucleotide and the Mg2+ ion. The eEF1Bα fragment (green) is clamped between domain 1 and 2 (cyan) but makes virtually no contacts to domain 3 (red).
Molecular Cell 2000 6, DOI: ( /S (00) )

3. Figure 2 Interaction of eEF1Bα with eEF1A
(A) Detailed stereo view of the insertion of eEF1Bα (gray, blue labels) between the switch 1 (upper left) and switch 2 (bottom right) of eEF1A (yellow, red labels). Blue lines represent selected intermolecular interactions. The C-terminal β strand of eEF1Bα with Lys-205b in the Mg2+ binding site is perpendicular to the page. Helices in eEF1A are marked with uppercase letters.
(B) Detailed stereo view of the interface with eEF1Bα (gray, blue labels) and domain 2 of eEF1A (yellow, red labels).
Molecular Cell 2000 6, DOI: ( /S (00) )

4. Figure 3
The Interface between eEF1A Domain 2 and eEF1Bα Overlaps with aa-tRNA Binding
(A) The CCA-aa end of tRNA (gold) superimposes with two loops of eEF1Bα (gray) when domain 2 (not shown) of the eEF1A:eEF1Bα complex is superimposed with domain 2 (not shown) of EF-Tu in complex with aa-tRNA.
(B) The flexibility of the loop demonstrated in the NMR structure may allow aa-tRNA to displace eEF1Bα. The NMR of eEF1Bα is shown yellow, the X-ray structure in gray, and the CCA-aa end of tRNA in gold. A space-filling representation of atoms in eEF1A within 10 Å of Phe-163b is shown in gray.
Molecular Cell 2000 6, DOI: ( /S (00) )