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TitleMovement of the biotin carboxylase B-domain as a result of ATP binding.
Journal, issue, pagesJ. Biol. Chem., Vol. 275, Page 16183-16190, Year 2000
Publish dateJan 19, 2000 (structure data deposition date)
AuthorsThoden, J.B. / Blanchard, C.Z. / Holden, H.M. / Waldrop, G.L.
External linksJ. Biol. Chem. / PubMed:10821865
MethodsX-ray diffraction
Resolution1.9 - 2.5 Å
Structure data

PDB-1dv1:
STRUCTURE OF BIOTIN CARBOXYLASE (APO)
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1dv2:
The structure of biotin carboxylase, mutant E288K, complexed with ATP
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • escherichia coli (E. coli)
KeywordsLIGASE / ATP-grasp / carboxylase / biotin-dependent / ATP-grasp biotin-dependent carboxylase

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