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Structure paper

TitleIn Human Pseudouridine Synthase 1 (hPus1), a C-Terminal Helical Insert Blocks tRNA from Binding in the Same Orientation as in the Pus1 Bacterial Homologue TruA, Consistent with Their Different Target Selectivities.
Journal, issue, pagesJ. Mol. Biol., Vol. 425, Page 3875-3887, Year 2013
Publish dateJan 11, 2013 (structure data deposition date)
AuthorsCzudnochowski, N. / Wang, A.L. / Finer-Moore, J. / Stroud, R.M.
External linksJ. Mol. Biol. / PubMed:23707380
MethodsX-ray diffraction
Resolution1.75 - 1.85 Å
Structure data

PDB-4iqm:
Crystal structure of the catalytic domain of human Pus1
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-4its:
Crystal structure of the catalytic domain of human Pus1 with MES in the active site
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-4j37:
Crystal structure of the catalytic domain of human Pus1
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-SO4:
SULFATE ION

ChemComp-CL:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

Source
  • homo sapiens (human)
KeywordsRNA BINDING PROTEIN / pseudouridine synthase / RNA modification / tRNA / pre-tRNA / steroid receptor RNA activator / U2 snRNA / beta sheet / isomerase

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