9YWN
Protein Structure of the First Glycoside Hydrolase Family 30, Subfamily 12 Endoxylanase
Summary for 9YWN
| Entry DOI | 10.2210/pdb9ywn/pdb |
| Descriptor | Glucuronoarabinoxylan endo-1,4-beta-xylanase, GLYCEROL, FORMIC ACID, ... (8 entities in total) |
| Functional Keywords | glycoside hydrolase, xylanase, endoxylanase, hydrolase |
| Biological source | Anaerobacterium chartisolvens |
| Total number of polymer chains | 6 |
| Total formula weight | 302381.12 |
| Authors | |
| Primary citation | St John, F.J.,Crooks, C.,Endres, M.,Pakdaman, L.,Koch, L.,Bynum, L.,Kuch, N.,Joachimiak, A.,Tan, K. Protein structure of a glycoside hydrolase family 30, subfamily 12 endo-1,4-beta-xylanase. Acta Crystallogr D Struct Biol, 82:370-382, 2026 Cited by PubMed Abstract: We have determined the X-ray crystallographic protein structure of endo-1,4-β-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. PubMed: 41870978DOI: 10.1107/S2059798326002160 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.916 Å) |
Structure validation
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