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Structure paper

TitleDiscovery of an ultraspecific triuret hydrolase (TrtA) establishes the triuret biodegradation pathway.
Journal, issue, pagesJ. Biol. Chem., Vol. 296, Page 100055-100055, Year 2020
Publish dateJun 22, 2020 (structure data deposition date)
AuthorsTassoulas, L.J. / Elias, M.H. / Wackett, L.P.
External linksJ. Biol. Chem. / PubMed:33172891
MethodsX-ray diffraction
Resolution1.45 - 2.1 Å
Structure data

PDB-6xix:
Triuret Hydrolase (TrtA) from Herbaspirillum sp. BH-1
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-6xj4:
Triuret Hydrolase (TrtA) from Herbaspirillum sp. BH-1 C162S bound with biuret
Method: X-RAY DIFFRACTION / Resolution: 1.78 Å

PDB-6xje:
Triuret Hydrolase (TrtA) from Herbaspirillum sp. BH-1 C162S bound with triuret
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

PDB-6xjm:
Biuret Hydrolase (BiuH) from Rhodococcus sp. Mel C169S bound with biuret
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-6xk1:
Biuret Hydrolase (BiuH) from Rhodococcus sp. Mel C169S Apo form
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-HOH:
WATER

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-C5J:
dicarbonimidic diamide

ChemComp-TIU:
tricarbonodiimidic diamide

Source
  • herbaspirillum sp. bh-1 (bacteria)
  • rhodococcus sp. mel (bacteria)
KeywordsHYDROLASE / TrtA / triuret / biuret / cysteine hydrolase / nitrogen / BiuH

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