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Structure paper

TitleCrystal contact-free conformation of an intrinsically flexible loop in protein crystal: Tim21 as the case study.
Journal, issue, pagesBiochim Biophys Acta Gen Subj, Vol. 1864, Page 129418-129418, Year 2020
Publish dateJun 7, 2019 (structure data deposition date)
AuthorsBala, S. / Shinya, S. / Srivastava, A. / Ishikawa, M. / Shimada, A. / Kobayashi, N. / Kojima, C. / Tama, F. / Miyashita, O. / Kohda, D.
External linksBiochim Biophys Acta Gen Subj / PubMed:31449839
MethodsX-ray diffraction / NMR (solution)
Resolution1.534 - 2 Å
Structure data

PDB-6k7d:
Crystal structure of MBPapo-Tim21 fusion protein with a 16-residue helical linker
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-6k7e:
Crystal structure of MBPapo-Tim21 fusion protein with a 17-residue helical linker
Method: X-RAY DIFFRACTION / Resolution: 1.534 Å

PDB-6k7f:
Crystal structure of MBPholo-Tim21 fusion protein with a 17-residue helical linker
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-6k8q:
Solution structure of the intermembrane space domain of the mitochondrial import protein Tim21 from S. cerevisiae
Method: SOLUTION NMR

Chemicals

ChemComp-HOH:
WATER

Source
  • escherichia coli (strain k12) (bacteria)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsSUGAR BINDING PROTEIN / TRANSLOCASE / MBP / Tim21 / fusion protein / helical linker / PROTEIN TRANSPORT / membrane / mitochondria / translocation

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