9ywn | pdb_00009ywn

Protein Structure of the First Glycoside Hydrolase Family 30, Subfamily 12 Endoxylanase

spinqualitylabelsall models 9ywn, resolution 1.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ywn is a 6 chain structure with sequence from Oscillospiraceae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.916Å Ligands: ACY, EDO, FMT, GOL, NA, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed We have determined the X-ray crystallographic protein structure of endo-1,4-beta-xylanase (EX) A from Anaerobacterium chartisolvens (AchXyn30A), a homologue of the recent biochemically characterized glycoside hydrolase family 30, subfamily 12 (GH30_12) EX from Acetivibrio clariflavus (AcXyn30B). The N-terminal GH30 catalytic domains (CDs) of these two enzymes share approximately 63% amino-acid sequence identity and the full-length proteins each consist of the GH30_12 CD, a family 6 carbohydrate-binding module and a C-terminal dockerin domain. In this report, we offer additional support for the recent subfamily classification of these EXs and provide detailed X-ray crystallographic protein structure analysis of AchXyn30A, the first protein structure from this newly defined GH30 subfamily. We also provide comparative structural analysis using a generated AcXyn30B homology model as well as other GH30 subfamily enzymes. Additionally, we examine potential xylan-chain interactions informed by the protein structure. These characterized EXs further illustrate the diversity of xylan-degrading enzymes which have evolved within glycoside hydrolase family 30. Protein structure of a glycoside hydrolase family 30, subfamily 12 endo-1,4-beta-xylanase.,St John FJ, Crooks C, Endres M, Pakdaman L, Koch L, Bynum L, Kuch N, Joachimiak A, Tan K Acta Crystallogr D Struct Biol. 2026 Apr 1;82(Pt 4):370-382. doi: , 10.1107/S2059798326002160. Epub 2026 Mar 23. PMID:41870978 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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