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. 2024 Jun 3;13:RP93686. doi: 10.7554/eLife.93686

Figure 2. Comparison of lauryl maltose neopentyl glycol (LMNG)-NConst and LMNG-NFlex structures.

(a) Overall superposition showing the movement of TM2 and the link between the N-terminus and TM1. LMNG-NConst in cyan and LMNG-NFlex in yellow (alternate subunits have been coloured in lighter shades). The KVRIEG motif has been coloured magenta with a sphere indicating the position of K125. The residues between the N-terminus and TM1 for the LMNG-NConst structure have been coloured blue. (b) As (a) but focussed on TM1. The conformation of TM1 differs between the two structures as seen by the change in position of Trp24. TM2’ is from the neighbouring subunit. HC denotes the hydrocarbon chain from a lipid. The positions of T86’ and L89’ of TM2 in the NFlex conformation are not compatible with F31 and I30 TM1 in the NConst conformation.

Figure 2.

Figure 2—video 1. Morph showing the conformational differences between structures of lauryl maltose neopentyl glycol (LMNG)-NConst and LMNG-NFlex.
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As the N-terminus and KVRIEG motif are not visible in the LMNG-NFlex structure, these residues are not present in the morph. Residues linking the N-terminal helix to TM1 are shown in blue. Trp24 is depicted by pink sticks.
Figure 2—video 2. Morph showing the conformational differences between structures of lauryl maltose neopentyl glycol (LMNG)-NConst and LMNG-NFlex.
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Focussed on TM1 with TM1, 2, 3, 4 of one subunit depicted in cyan, green, yellow, and red respectively and TM2 of a second subunit in darker green. The movement of TM2 stems from the region around Phe 83 so that the position of the Cα atom of Lys103 near the top of TM2 of the respective structures differs by ~8.5 Å.