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. Author manuscript; available in PMC: 2023 Aug 4.
Published in final edited form as: Structure. 2022 May 20;30(8):1157–1168.e3. doi: 10.1016/j.str.2022.04.013

Table 2.

Conformational transitions of membrane proteins modeled with experimental EPR DEER distance restraints.

Protein (Organism) Starting Conformation (PDB ID) Target Conformation (PDB ID) No of Restraints No of helical Residues modeled References
Rhodopsin (Bos taurus) Active (2X72) Inactive (1GZM) 10 96 (Li et al., 2004; Standfuss et al., 2011)
Rhodopsin Inactive (1GZM) Active (2X72) 10 96
LeuT (Aquifex aeolicus) Inward-facing (3TT3) Outward-facing (2A65) 11 167 (Kazmier et al., 2014a; Krishnamurthy and Gouaux, 2012; Yamashita et al., 2005)
vSGLT (Vibrio parahaemolyticus) Outward-opena (5NV9) Substrate free (2XQ2) 11 241 (Paz et al., 2018; Wahlgren et al., 2018; Watanabe et al., 2010)
Mhp1 (Microbacterium liquefaciens) Outward-facing (2JLN) Inward-facing (2X79) 14 209 (Shimamura et al., 2010; Weyand et al., 2008)
Mhp1 Inward-facing (2X79) Outward-facing (2JLN) 14 201
a

The vSGLT OF conformation was generated from the X-ray structure of the homolog SiaT.