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Figure 2 | BMC Structural Biology

Figure 2

From: Multiple molecular dynamics simulation of the isoforms of human translation elongation factor 1A reveals reversible fluctuations between "open" and "closed" conformations and suggests specific for eEF1A1 affinity for Ca2+-calmodulin

Figure 2

Ribbon representation of the eEF1A molecule. a – domains I, II and III; 1 and 2 – amino acid residues Arg69-Leu77 and His295-Gly305, which are on the surface of the gap between the domains I and II, 3 and 4 – motifs Asn311-Gly327 and Gly422-Val437, suggested to be the calmodulin binding site in eEF1A1. b – amino acid residues with a positive difference between the rmsf of eEF1A2 and eEF1A1 of more than 0.02 nm (Met1-Lys5, Asp35-Glu48, Gly50-Thr58, Asp61, Lys62, Lys64-Glu68, Gly70-Asp74, Ala125-Ser128, Val216-Gly221, Ala223, Cys/Thr234, Gly258, Ile259, Pro282, His296-Ala298, Ser316, M3l318-Arg322, Gln352, His364, Thr365, Tyr418-Pro420, ribbon colored in red) and with negative differences of less than -0.02 nm (Asn130, Ser157, Lys313, Ser329, Ser383, Gly384, Glu388, Asp398, ribbon colored in blue); side chains of residues Asp197 and Mly55 which stabilize the motif Asp35-Asp74 in eEF1A1 are shown.

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BMC Structural Biology

ISSN: 1472-6807

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