Skip to main content
Fig. 4 | Biotechnology for Biofuels

Fig. 4

From: The xyl-doc gene cluster of Ruminiclostridium cellulolyticum encodes GH43- and GH62-α-l-arabinofuranosidases with complementary modes of action

Fig. 4

Overall structure modeling of GH4316-1229, GH4310-1233 and GH62-1234. Models established using the server Phyre2 are shown in this figure. The ProQ2 (Phyre 2 server) quality assessment was checked for each model. Quality scores obtained with SWISS-MODEL and RaptorX were determined for each model. a The 3D structure of the catalytic module of the protein GH4316-1229 was built using the 3D structure of Ct43Araf (PDB ID: 5a8d.1.A) from Clostridium thermocellum. In red, the catalytic aspartate D40; in purple, the aspartate “helper” D159,; and in green, the catalytic glutamate E208. (SWISS-MODEL quality scores: GMQE = 0.8, QMEAN = − 2.33; RaptorX quality scores: P = 5.6710−15, uGDT(GDT) = 273 (88). b The structure of the N-terminal part (GH43-X19) of GH4310-1233 was modeled on the basis of the 3D structure of HiAXHd3 (PDB ID: 3zxl.A) from Humicola insolens. In red, the catalytic aspartate D46; in purple, the aspartate “helper” D156; and in green, the catalytic glutamate E207. The X19 module is colored in yellow. (SWISS-MODEL quality scores: GMQE = 0.7, QMEAN = − 4.5; RaptorX quality scores: P = 3.3610−19, uGDT(GDT) = 325 (61). c For both GH62 catalytic modules (GH62-1234 and GH62-CE6-1240), the template used was the GH62-α-l-ABFs from Coprinopsis cinerea (PDB ID: 5b6s.1.A). In red, the catalytic aspartate D57; in purple, the aspartate “helper” D163; and in green, the catalytic glutamate E213. (SWISS-MODEL quality scores: GMQE = 0.7, QMEAN = − 3.94; RaptorX quality scores: P = 1.1210−10, uGDT(GDT) = 210 (67)

Back to article page