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Structure paper

TitleDomain swapping dissection in Thermotoga maritima arginine binding protein: How structural flexibility may compensate destabilization.
Journal, issue, pagesBiochim. Biophys. Acta, Vol. 1866, Page 952-962, Year 2018
Publish dateMay 3, 2018 (structure data deposition date)
AuthorsSmaldone, G. / Berisio, R. / Balasco, N. / D'Auria, S. / Vitagliano, L. / Ruggiero, A.
External linksBiochim. Biophys. Acta / PubMed:29860047
MethodsX-ray diffraction
Resolution1.03 - 2.69 Å
Structure data

PDB-6ggp:
Structure of the ligand-free form of truncated ArgBP (residues 20-233) from T. maritima
Method: X-RAY DIFFRACTION / Resolution: 1.03 Å

PDB-6ggv:
Structure of the arginine-bound form of truncated (residues 20-233) ArgBP from T. maritima
Method: X-RAY DIFFRACTION / Resolution: 2.69 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-ARG:
ARGININE

ChemComp-CD:
Unknown entry

Source
  • thermotoga maritima (strain atcc 43589 / msb8 / dsm 3109 / jcm 10099) (bacteria)
  • thermotoga maritima (bacteria)
KeywordsTRANSPORT PROTEIN / Domain swapping / Biosensors / Argininemia diagnosis / Protein structure-stability / Calorimetry. / Calorimetry

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