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Structure paper

TitleThe beta-hairpin from the Thermus thermophilus HB27 laccase works as a pH-dependent switch to regulate laccase activity.
Journal, issue, pagesJ. Struct. Biol., Vol. 213, Page 107740-107740, Year 2021
Publish dateAug 7, 2019 (structure data deposition date)
AuthorsMiranda-Blancas, R. / Avelar, M. / Rodriguez-Arteaga, A. / Sinicropi, A. / Rudino-Pinera, E.
External linksJ. Struct. Biol. / PubMed:33962016
MethodsX-ray diffraction
Resolution1.702 - 1.813 Å
Structure data

PDB-6q29:
Crystal structure of Laccase from Thermus thermophilus HB27 with an open conformation of beta-hairpin (Average deposted dose 2.5 MGy)
Method: X-RAY DIFFRACTION / Resolution: 1.702 Å

PDB-6tyr:
Crystal structure of Laccase from Thermus thermophilus HB27 with a close conformation of its beta-hairpin
Method: X-RAY DIFFRACTION / Resolution: 1.813 Å

Chemicals

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-CU:
COPPER (II) ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-CIT:
CITRIC ACID

Source
  • thermus thermophilus (strain hb27 / atcc baa-163 / dsm 7039) (bacteria)
KeywordsSTRUCTURAL PROTEIN / open loop / multicopper oxidase / OXIDOREDUCTASE / close loop / laccase

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