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TitleCMT disease severity correlates with mutation-induced open conformation of histidyl-tRNA synthetase, not aminoacylation loss, in patient cells.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Year 2019
Publish dateJun 16, 2017 (structure data deposition date)
AuthorsBlocquel, D. / Sun, L. / Matuszek, Z. / Li, S. / Weber, T. / Kuhle, B. / Kooi, G. / Wei, N. / Baets, J. / Pan, T. ...Blocquel, D. / Sun, L. / Matuszek, Z. / Li, S. / Weber, T. / Kuhle, B. / Kooi, G. / Wei, N. / Baets, J. / Pan, T. / Schimmel, P. / Yang, X.L.
External linksProc. Natl. Acad. Sci. USA / PubMed:31501329
MethodsX-ray diffraction
Resolution2.787 - 3.696 Å
Structure data

PDB-5w6m:
Crystal structure of the human histidyl-tRNA synthetase mutant D175E
Method: X-RAY DIFFRACTION / Resolution: 3.696 Å

PDB-6o76:
Human cytosolic Histidyl-tRNA synthetase (HisRS) with WHEP domain
Method: X-RAY DIFFRACTION / Resolution: 2.787 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLIGASE / tRNA-synthetase / CMT mutant / tRNA / CMT / WHEP domain / alpha beta domain

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