4pva | pdb_00004pva

Crystal structure of GH62 hydrolase from thermophilic fungus Scytalidium thermophilum

spinqualitylabelsall models 4pva, resolution 1.23Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pva is a 1 chain structure with sequence from Mycothermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.23Å Ligands: GOL, MSE, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A059U759_9PEZI Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from arabinoxylan.[ARBA:ARBA00025637][RuleBase:RU368117] Publication Abstract from PubMed The genome of the thermophilic fungus Scytalidium thermophilum (strain CBS 625.91) harbours a wide range of genes involved in carbohydrate degradation, including three genes, abf62A, abf62B and abf62C, predicted to encode glycoside hydrolase family 62 (GH62) enzymes. Transcriptome analysis showed that only abf62A and abf62C are actively expressed during growth on diverse substrates including straws from barley, alfalfa, triticale and canola. The abf62A and abf62C genes were expressed in Escherichia coli and the resulting recombinant proteins were characterized. Calcium-free crystal structures of Abf62C in apo and xylotriose bound forms were determined to 1.23 and 1.48 A resolution respectively. Site-directed mutagenesis confirmed Asp55, Asp171 and Glu230 as catalytic triad residues, and revealed the critical role of non-catalytic residues Asp194, Trp229 and Tyr338 in positioning the scissile alpha-L-arabinofuranoside bond at the catalytic site. Further, the +2R substrate-binding site residues Tyr168 and Asn339, as well as the +2NR residue Tyr226, are involved in accommodating long-chain xylan polymers. Overall, our structural and functional analysis highlights characteristic differences between Abf62A and Abf62C, which represent divergent subgroups in the GH62 family. Functional and structural diversity in GH62 alpha-L-arabinofuranosidases from the thermophilic fungus Scytalidium thermophilum.,Kaur AP, Nocek BP, Xu X, Lowden MJ, Leyva JF, Stogios PJ, Cui H, Di Leo R, Powlowski J, Tsang A, Savchenko A Microb Biotechnol. 2014 Sep 29. doi: 10.1111/1751-7915.12168. PMID:25267315 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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