5ufv | pdb_00005ufv

Crystal Structure of a Cellulose-active Polysaccharide Monooxygenase from M. thermophila (MtPMO3*)

spinqualitylabelsall models 5ufv, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ufv is a 6 chain structure with sequence from Thermothelomyces thermophilus ATCC 42464. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.45Å Ligands: CU, HIC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G2QAB5_MYCTT Publication Abstract from PubMed Polysaccharide monooxygenases (PMOs) are secreted metalloenzymes that catalyze the oxidative degradation of polysaccharides in a copper-, oxygen-, and reductant-dependent manner. Cellulose-active fungal PMOs degrade cellulosic substrates to be utilized as a carbon source for fungal growth. To gain insight into the PMO mechanism, the role of conserved residues in the copper coordination sphere was investigated. Here, we report active-site hydrogen-bonding motifs in the secondary copper coordination sphere of MtPMO3*, a C1-oxidizing PMO from the ascomycete fungus Myceliophthora thermophila. A series of point substitutions that disrupt this conserved network are used to interrogate its function. Activity assays, in conjunction with EPR spectroscopy, demonstrate that residues H161 and Q167 are involved in stabilizing bound oxygen, and H161 appears to play a role in proton transfer. Additionally, Q167 increases the ligand donor strength of Y169 to the copper via a hydrogen-bonding interaction. Altogether, H161 and Q167 are important for oxygen activation, and the results are suggestive of a copper-oxyl active intermediate. The Role of the Secondary Coordination Sphere in a Fungal Polysaccharide Monooxygenase.,Span EA, Suess DL, Deller MC, Britt RD, Marletta MA ACS Chem Biol. 2017 Mar 3. doi: 10.1021/acschembio.7b00016. PMID:28257189 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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