Table 1.
Available structural models of VMATs
NamePMDB codeTemplateIdentityConformationProQM scoreReference
   %    
Ccyt N/A LacY 1PV6 ∼12a Cytoplasm facing 0.561 Vardy et al., 2004  
Ccyt’ PM0078823 LacY 1PV7 ∼12 Cytoplasm facing 0.616 Yaffe et al., 2013  
Clum PM0078824 LacY 1PV7-RSM ∼12 Lumen facing 0.616 Yaffe et al., 2013  
Clum’ PM0080553 YajR 3WDO ∼18 Lumen facing 0.717 Yaffe et al., 2016  
NamePMDB codeTemplateIdentityConformationProQM scoreReference
   %    
Ccyt N/A LacY 1PV6 ∼12a Cytoplasm facing 0.561 Vardy et al., 2004  
Ccyt’ PM0078823 LacY 1PV7 ∼12 Cytoplasm facing 0.616 Yaffe et al., 2013  
Clum PM0078824 LacY 1PV7-RSM ∼12 Lumen facing 0.616 Yaffe et al., 2013  
Clum’ PM0080553 YajR 3WDO ∼18 Lumen facing 0.717 Yaffe et al., 2016  

Structural models of rat VMAT2 have been reported in two alternate conformations. Three of these are available from the Protein Model Database (PMDB; Castrignanò et al., 2006). The models were built using different x-ray structure templates and, in one case (Clum), a repeat-swapped model as a template; the underlying sequence alignments also differ. Identity: the percentage of identical residues in the target and template sequences in the region of the target that was modeled. The structural quality of the models is estimated by the ProQM score, which takes values of 0 to 1, and where higher values indicate better consistency with known structures (Ray et al., 2010). For reference, the ProQM scores of the templates are 0.729 (Protein Data Bank accession no. 1PV7) and 0.741 (Protein Data Bank accession no. 3WDO). N/A, not applicable.

a

For the Ccyt model, the sequence identity was estimated from a TMalign structural alignment of the model to its template.

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