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Structure paper

TitleThe C-terminal domain conformational switch revealed by the crystal structure of malyl-CoA lyase from Roseiflexus castenholzii.
Journal, issue, pagesBiochem. Biophys. Res. Commun., Vol. 518, Page 72-79, Year 2019
Publish dateJul 19, 2019 (structure data deposition date)
AuthorsTang, W. / Wang, Z. / Zhang, C. / Wang, C. / Min, Z. / Zhang, X. / Liu, D. / Shen, J. / Xu, X.
External linksBiochem. Biophys. Res. Commun. / PubMed:31405562
MethodsX-ray diffraction
Resolution2.527 - 2.64 Å
Structure data

PDB-6kin:
Crystal structure of the tri-functional malyl-CoA lyase from Roseiflexus castenholzii
Method: X-RAY DIFFRACTION / Resolution: 2.527 Å

PDB-6kkh:
Crystal structure of the oxalate bound malyl-CoA lyase from Roseiflexus castenholzii
Method: X-RAY DIFFRACTION / Resolution: 2.64 Å

Chemicals

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

ChemComp-HOH:
WATER

ChemComp-OXL:
OXALATE ION

ChemComp-MG:
Unknown entry

Source
  • roseiflexus castenholzii (strain dsm 13941 / hlo8) (bacteria)
KeywordsLYASE / Malyl-CoA lyase / CitE-like superfamily / Roseiflexus castenholzii / Conformational changes

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