4pmu

Crystal structure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P1211)

spinqualitylabelsall models 4pmu, resolution 2.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pmu is a 6 chain structure with sequence from Xanthomonas citri pv. citri str. 306. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.857Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8PEU1_XANAC Publication Abstract from PubMed Xanthomonas pathogens attack a variety of economically-relevant plants and their xylan CUT system (Carbohydrate Utilization with TonB-dependent outer membrane transporter system) contains two major xylanase-related genes, XynA and XynB, which influence biofilm formation and virulence by molecular mechanisms still elusive. Herein, we demonstrated that XynA is a rare reducing-end xylose-releasing exo-oligoxylanase and not an endo-beta-1,4-xylanase as predicted. Structural analysis revealed that an insertion in the beta7-alpha7 loop induces dimerization and promotes a physical barrier at the +2 subsite conferring this unique mode of action within the GH10 family. A single mutation that impaired dimerization became XynA active against xylan and high endolytic activity was achieved when this loop was tailored to match a canonical sequence of endo-beta-1,4-xylanases, supporting our mechanistic model. On the other hand, the divergent XynB showed to be a classical endo-beta-1,4-xylanase, despite the low sequence similarity to characterized GH10 xylanases. Interestingly, this enzyme contains a calcium ion bound nearby to the glycone-binding region, which is required for catalytic activity and structural stability. These results shed light on the molecular basis for xylan degradation by Xanthomonas and suggest how these enzymes synergistically assist infection and pathogenesis. Our findings indicate that XynB contributes to breach the plant cell-wall barrier providing nutrients and facilitating the translocation of effector molecules, whereas the exo-oligoxylanase XynA possibly participates in the suppression of oligosaccharide-induced immune responses. Molecular mechanisms associated with xylan degradation by Xanthomonas plant pathogens.,Santos CR, Hoffmam ZB, Martins VP, Zanphorlin LM, Assis LH, Honorato RV, Oliveira PS, Ruller R, Murakami MT J Biol Chem. 2014 Sep 29. pii: jbc.M114.605105. PMID:25266726 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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