Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6JGO

Crystal structure of barley exohydrolaseI W434H mutant in complex with 4I,4III,4V-S-trithiocellohexaose

Summary for 6JGO
Entry DOI10.2210/pdb6jgo/pdb
Related PRD IDPRD_900034
DescriptorBETA-D-GLUCAN GLUCOHYDROLASE ISOENZYME EXO1, beta-D-glucopyranose-(1-4)-4-thio-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
Functional Keywordsbarley exohydrolasei, hydrolase, enzyme function
Biological sourceHordeum vulgare subsp. vulgare (Domesticated barley)
Total number of polymer chains1
Total formula weight68519.61
Authors
Luang, S.,Streltsov, V.A.,Hrmova, M. (deposition date: 2019-02-14, release date: 2020-08-19, Last modification date: 2024-11-06)
Primary citationLuang, S.,Fernandez-Luengo, X.,Nin-Hill, A.,Streltsov, V.A.,Schwerdt, J.G.,Alonso-Gil, S.,Ketudat Cairns, J.R.,Pradeau, S.,Fort, S.,Marechal, J.D.,Masgrau, L.,Rovira, C.,Hrmova, M.
The evolutionary advantage of an aromatic clamp in plant family 3 glycoside exo-hydrolases.
Nat Commun, 13:5577-5577, 2022
Cited by
PubMed Abstract: In the barley β-D-glucan glucohydrolase, a glycoside hydrolase family 3 (GH3) enzyme, the Trp286/Trp434 clamp ensures β-D-glucosides binding, which is fundamental for substrate hydrolysis during plant growth and development. We employ mutagenesis, high-resolution X-ray crystallography, and multi-scale molecular modelling methods to examine the binding and conformational behaviour of isomeric β-D-glucosides during substrate-product assisted processive catalysis that operates in GH3 hydrolases. Enzyme kinetics reveals that the W434H mutant retains broad specificity, while W434A behaves as a strict (1,3)-β-D-glucosidase. Investigations of reactant movements on the nanoscale reveal that processivity is sensitive to mutation-specific alterations of the tryptophan clamp. While wild-type and W434H utilise a lateral cavity for glucose displacement and sliding of (1,3)-linked hydrolytic products through the catalytic site without dissociation, consistent with their high hydrolytic rates, W434A does not adopt processive catalysis. Phylogenomic analyses of GH3 hydrolases disclose the evolutionary advantage of the tryptophan clamp that confers broad specificity, high catalytic efficiency, and processivity.
PubMed: 36151080
DOI: 10.1038/s41467-022-33180-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

227111

數據於2024-11-06公開中

PDB statisticsPDBj update infoContact PDBjnumon