Fig. 5: Structural comparisons between G. haemolysans IgA1P and S. pneumoniae IgA1P complexes with IgA1.
From: A substrate-induced gating mechanism is conserved among Gram-positive IgA1 metalloproteases
a The G. haemolysans IgA1P-E1848A/IgA1 complex is shown (colored) superimposed on the S. pneumoniae IgA1P-E1605A/IgA1 complex (white). b Blow-up of the region that includes the NTD2 domains and active site loops. c RMSDs between the two metallo-IgA1Ps in their substrate free (black) and substrate-bound state (red). d RMSDs between the two bound IgA1 HCs within their respective metallo-IgA1P. e Blow-up of the active sites with the conserved metalloprotease motif in the bound states. The G. haemolysans IgA1P glutamic acid residues (red) and histidine residues (blue) are shown along with their counterparts within the S. pneumoniae IgA1P (white). f Blow-up of the active site loops show missing density in the IgA1-bound G. haemolysans IgA1P-E1848A for residues 1298-1307 and S. pneumoniae IgA1P-E1605A for residues 1054-1063. g Catalytic proficiencies are compared between G. haemolysans IgA1P and the G. haemolysans IgA1P Δ1297-1306 mutant.
