6krn | pdb_00006krn

Crystal structure of GH30 xylanase B from Talaromyces cellulolyticus expressed by Pichia pastoris in complex with aldotriuronic acid

spinqualitylabelsall models 6krn, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6krn is a 1 chain structure with sequence from Saccharomyces uvarum and Talaromyces cellulolyticus CF-2612. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.653Å Ligands: BMA, GCV, MAN, NAG, XYP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A510NXC4_TALPI Publication Abstract from PubMed Xylanase B, a member of subfamily 7 of the GH30 (glycoside hydrolase family 30) from Talaromyces cellulolyticus (TcXyn30B), is a bifunctional enzyme with glucuronoxylanase and xylobiohydrolase activities. In the present study, crystal structures of the native enzyme and the enzyme-product complex of TcXyn30B expressed in Pichia pastoris were determined at resolutions of 1.60 and 1.65 A, respectively. The enzyme complexed with 2(2) -(4-O-methyl-alpha-d-glucuronyl)-xylobiose (U(4m2) X) revealed that TcXyn30B strictly recognizes both the C-6 carboxyl group and the 4-O-methyl group of the 4-O-methyl-alpha-d-glucuronyl side chain by the conserved residues in GH30-7 endoxylanases. The crystal structure and site-directed mutagenesis indicated that Asn-93 on the beta2-alpha2-loop interacts with the non-reducing end of the xylose residue at subsite-2 and is likely to be involved in xylobiohydrolase activity. These findings provide structural insight into the mechanisms of substrate recognition of GH30-7 glucuronoxylanase and xylobiohydrolase. Substrate recognition by a bifunctional GH30-7 xylanase B from Talaromyces cellulolyticus.,Nakamichi Y, Watanabe M, Matsushika A, Inoue H FEBS Open Bio. 2020 Jun;10(6):1180-1189. doi: 10.1002/2211-5463.12873. Epub 2020 , May 22. PMID:32359208 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA