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TitleA conserved pi-helix plays a key role in thermoadaptation of catalysis in the glycoside hydrolase family 4.
Journal, issue, pagesBiochim Biophys Acta Proteins Proteom, Vol. 1869, Page 140523-140523, Year 2021
Publish dateMar 26, 2020 (structure data deposition date)
AuthorsMohapatra, S.B. / Manoj, N.
External linksBiochim Biophys Acta Proteins Proteom / PubMed:32853774
MethodsX-ray diffraction
Resolution1.95 Å
Structure data

PDB-7br4:
Structure of deletion mutant of alpha-glucuronidase (TM0752) from Thermotoga maritima
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

ChemComp-HOH:
WATER

Source
  • thermotoga maritima (strain atcc 43589 / msb8 / dsm 3109 / jcm 10099) (bacteria)
KeywordsHYDROLASE / hydrolase-oxidoreductase / alpha-glucuronidase activity / carbohydrate metabolism / NAD-binding Rossmann-fold / LDH C-terminal domain-like

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