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Structure paper

TitleIdentification of structural transitions in bacterial fatty acid binding proteins that permit ligand entry and exit at membranes.
Journal, issue, pagesJ. Biol. Chem., Vol. 298, Page 101676-101676, Year 2022
Publish dateSep 17, 2018 (structure data deposition date)
AuthorsGullett, J.M. / Cuypers, M.G. / Grace, C.R. / Pant, S. / Subramanian, C. / Tajkhorshid, E. / Rock, C.O. / White, S.W.
External linksJ. Biol. Chem. / PubMed:35122790
MethodsX-ray diffraction
Resolution1.6 - 2.35 Å
Structure data

PDB-6mh9:
The crystal structure of the Staphylococcus aureus Fatty acid Kinase (Fak) B1 protein A121I mutant to 2.02 Angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 2.02 Å

PDB-6nm1:
The crystal structure of the Staphylococcus aureus Fatty acid Kinase (Fak) B1 protein A158L mutant to 2.33 Angstrom resolution exhibits a conformation change compared to the wild type form
Method: X-RAY DIFFRACTION / Resolution: 2.33 Å

PDB-7scl:
The X-ray crystal structure of Staphylococcus aureus Fatty Acid Kinase B1 (FakB1) mutant R173A in complex with Palmitate to 1.60 Angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-7sg3:
The X-ray crystal structure of the Staphylococcus aureus Fatty Acid Kinase B1 mutant A121I-A158L to 2.35 Angstrom resolution (Open form chain A, Palmitate bound)
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

Chemicals

ChemComp-PLM:
PALMITIC ACID

ChemComp-HOH:
WATER

ChemComp-MYR:
MYRISTIC ACID

ChemComp-GOL:
GLYCEROL

Source
  • staphylococcus aureus (bacteria)
KeywordsTRANSFERASE / Staphylococcus aureus / FakB1 / mutant TRANSFERASE / mutant / conformation change / TRANSFERASE/SUBSTRATE / Fatty acid kinase B1 / Fatty acid transporter / TRANSFERASE-SUBSTRATE complex / Fatty acid kinase A / phosphorylation / fatty acid / N-terminus domain / LIGASE

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