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Structure paper

TitleMolecular mechanism underlying high-affinity terephthalate binding and conformational change of TBP from Ideonella sakaiensis.
Journal, issue, pagesInt. J. Biol. Macromol., Vol. 243, Page 125252-125252, Year 2023
Publish dateNov 25, 2022 (structure data deposition date)
AuthorsLee, S.H. / Seo, H. / Hong, H. / Kim, M. / Kim, K.J.
External linksInt. J. Biol. Macromol. / PubMed:37295700
MethodsX-ray diffraction
Resolution1.02 - 2 Å
Structure data

PDB-8hk9:
Apo-form of Periplasmic terephthalate binding protein (TBP) from Ideonella sakaiensis
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-8hka:
TPA bound-form of Periplasmic terephthalate binding protein (TBP) from Ideonella sakaiensis
Method: X-RAY DIFFRACTION / Resolution: 1.02 Å

PDB-8hkb:
TPA bound-form of Periplasmic terephthalate binding protein (TBP) from Ideonella sakaiensis mutant K184D
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-UB7:
terephthalic acid

Source
  • ideonella sakaiensis (bacteria)
KeywordsTRANSPORT PROTEIN / Periplasmic protein / Terephthalate binding protein / transportation protein / Ideonella sakaiensis

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