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Structure paper

TitleA single aromatic core mutation converts a designed "primitive" protein from halophile to mesophile folding.
Journal, issue, pagesProtein Sci., Vol. 24, Page 27-37, Year 2015
Publish dateJun 9, 2014 (structure data deposition date)
AuthorsLongo, L.M. / Tenorio, C.A. / Kumru, O.S. / Middaugh, C.R. / Blaber, M.
External linksProtein Sci. / PubMed:25297559
MethodsX-ray diffraction
Resolution1.7 - 1.746 Å
Structure data

PDB-4qkr:
Crystal Structure of 6xTyr/PV2: de novo designed beta-trefoil architecture with symmetric primary structure (L22Y/L44Y/L64Y/L85Y/L108Y/L132Y, Primitive Version 2)
Method: X-RAY DIFFRACTION / Resolution: 1.746 Å

PDB-4qks:
Crystal Structure of 6xTrp/PV2: de novo designed beta-trefoil architecture with symmetric primary structure (L22W/L44W/L64W/L85W/L108W/L132W his Primitive Version 2)
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-IMD:
IMIDAZOLE

ChemComp-HOH:
WATER

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-SO4:
SULFATE ION

Source
  • synthetic (others)
KeywordsDE NOVO PROTEIN / simplified protein design / prebiotic protein / beta-trefoil

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