This PDF file includes:

• Table S1. Data collection, phasing, and refinement statistics for first structural determination of PcCel45A.
• Table S2. Statistics of data collection and refinement of the x-ray structure of PcCel45A WT with and without 5M cellopentaose at cryogenic temperature.
• Table S3. Statistics of data collection and refinement of the x-ray structure of PcCel45A N92D with and without cellopentaose at cryogenic temperature and PcCel45A N92D unliganded structure at room temperature.
• Table S4. Statistics of data collection and refinement of the x-ray structure of PcCel45A D114N with and without 5 mM cellopentaose at cryogenic temperature.
• Table S5. Statistics of data collection and refinement of the neutron and x-ray structure of PcCel45A WT unliganded.
• Table S6. Statistics of data collection and refinement of the neutron and x-ray structure of PcCel45A WT with 2.5 mM cellopentaose.
• Table S7. Statistics of data collection and refinement of the x-ray structure of PcCel45A N105D.
• Fig. S1. Determination of anomeric forms of products.
• Fig. S2. Structural comparison of PcCel45A with other GH45 enzymes.
• Fig. S3. Activity profile of PcCel45A WT and mutants.
• Fig. S4. Temperature effect on PcCel45A structure.
• Fig. S5. Substrate recognition of PcCel45A WT and mutants.
• Fig. S6. Joint refined structure of PcCel45A WT with 2.5 mM cellopentaose.
• Fig. S7. Neighboring pair residues in the proton relay pathway.
• Fig. S8. Structural and activity profile of PcCel45A N105D mutant.
• Fig. S9. SDS-PAGE and Native-PAGE of PcCel45A WT and mutants.
• Legend for movie S1

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Other Supplementary Material for this manuscript includes the following:

• Movie S1 (.m4v format). The proposed proton relay pathway between Asp⁹² (general base) and Asn¹¹⁴ (general acid) residues in PcCel45A.