7w8m | pdb_00007w8m

Crystal structure of Co-type nitrile hydratase mutant from Pseudomonas thermophila - A129R

spinqualitylabelsall models 7w8m, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7w8m is a 2 chain structure with sequence from Pseudonocardia thermophila and Pseudonocardia thermophila DSM 43832. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: CO, CSD, CSO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NHAA_PSETH NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. Publication Abstract from PubMed The narrow substrate scope limits the wide industrial application of enzymes. Here, we successfully broadened the substrate scope of a nitrile hydratase (NHase) through mutation of two tunnel entrance residues based on rational tunnel calculation. Two variants, with increased specific activity, especially toward bulky substrates, were obtained. Crystal structure analysis revealed that the mutations led to the expansion of the tunnel entrance, which might be conducive to substrate entry. More importantly, molecular dynamics simulations illustrated that the mutations introduced anti-correlated movements to the regions around the substrate tunnel and the active site, which would promote substrate access during the dynamic process of catalysis. Additionally, mutations on the corresponding tunnel entrance residues on other NHases also enhanced their activity toward bulky substrates. These results not only revealed that residues located at the enzyme surface were a key factor in enzyme catalytic performance, but also provided dynamic evidence for insight into enzyme substrate scope broadening. Insight into the broadened substrate scope of nitrile hydratase by static and dynamic structure analysis.,Ma D, Cheng Z, Peplowski L, Han L, Xia Y, Hou X, Guo J, Yin D, Rao Y, Zhou Z Chem Sci. 2022 Jul 6;13(28):8417-8428. doi: 10.1039/d2sc02319a. eCollection 2022 , Jul 20. PMID:35919716 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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