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Structure paper

TitleClosed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity.
Journal, issue, pagesJ. Mol. Biol., Vol. 334, Page 1023-1041, Year 2003
Publish dateSep 29, 2003 (structure data deposition date)
AuthorsAparicio, R. / Ferreira, S.T. / Polikarpov, I.
External linksJ. Mol. Biol. / PubMed:14643664
MethodsX-ray diffraction
Resolution1.5 - 2.85 Å
Structure data

PDB-1r2r:
CRYSTAL STRUCTURE OF RABBIT MUSCLE TRIOSEPHOSPHATE ISOMERASE
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-1r2s:
CRYSTAL STRUCTURE OF RABBIT MUSCLE TRIOSEPHOSPHATE ISOMERASE
Method: X-RAY DIFFRACTION / Resolution: 2.85 Å

PDB-1r2t:
CRYSTAL STRUCTURE OF RABBIT MUSCLE TRIOSEPHOSPHATE ISOMERASE
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

Chemicals

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-MG:
Unknown entry

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

ChemComp-HOH:
WATER

Source
  • oryctolagus cuniculus (rabbit)
KeywordsISOMERASE / TIM; Closed loop conformation in the ligand-free state; Conformational heterogeneity; Tim-barrel

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