2yet | pdb_00002yet

THERMOASCUS GH61 ISOZYME A

spinqualitylabelsall models 2yet, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2yet is a 2 chain structure with sequence from Thermoascus aurantiacus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACE, CU, GOL, NAG NonStd Res: HIC Related: 3zud Activity: Cellulase, with EC number 3.2.1.4 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The enzymatic degradation of recalcitrant plant biomass is one of the key industrial challenges of the 21st century. Accordingly, there is a continuing drive to discover new routes to promote polysaccharide degradation. Perhaps the most promising approach involves the application of "cellulase-enhancing factors," such as those from the glycoside hydrolase (CAZy) GH61 family. Here we show that GH61 enzymes are a unique family of copper-dependent oxidases. We demonstrate that copper is needed for GH61 maximal activity and that the formation of cellodextrin and oxidized cellodextrin products by GH61 is enhanced in the presence of small molecule redox-active cofactors such as ascorbate and gallate. By using electron paramagnetic resonance spectroscopy and single-crystal X-ray diffraction, the active site of GH61 is revealed to contain a type II copper and, uniquely, a methylated histidine in the copper's coordination sphere, thus providing an innovative paradigm in bioinorganic enzymatic catalysis. Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components.,Quinlan RJ, Sweeney MD, Lo Leggio L, Otten H, Poulsen JC, Johansen KS, Krogh KB, Jorgensen CI, Tovborg M, Anthonsen A, Tryfona T, Walter CP, Dupree P, Xu F, Davies GJ, Walton PH Proc Natl Acad Sci U S A. 2011 Sep 13;108(37):15079-84. Epub 2011 Aug 29. PMID:21876164 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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