TY - JOUR
T1 - Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog
AU - Chook, Yuh Min
AU - Ke, Hengming
AU - Lipscomb, William N.
PY - 1993/9/15
Y1 - 1993/9/15
N2 - We have solved the structure of a chorismate mutase (chorismate pyruvatemutase, EC 5.4.99.5), the 1.9-Å crystal structure of the monofunctional enzyme from Bacillus subtilis. The structure determination process was an unusual one, involving 12 monomers of the enzyme in the asymmetric unit. This structure was solved by the multiple isomorphous replacement method with partial structure phase combination and molecular averaging. The final model, which includes 1380 residues and 522 water molecules in an asymmetric unit, has been refined at 1.9 Å and the current crystallographic R value is 0.201. The B. subtilis chorismate mutase is a homotrimer, with β-sheets from each monomer packing to form the core of a pseudo-αβ-barrel with helices on the outside of the trimer. In addition, the active sites have been located by using data from a complex with an endo-oxabicyclic inhibitor that mimics the transition state of the reaction. The structure of this complex has been refined to 2.2 Å with a current R value of 0.182 for a model that includes 1388 residues, 12 inhibitor molecules, and 530 water molecules in the asymmetric unit. In each trimer, three equivalent active sites are located at the interfaces of two adjacent summits.
AB - We have solved the structure of a chorismate mutase (chorismate pyruvatemutase, EC 5.4.99.5), the 1.9-Å crystal structure of the monofunctional enzyme from Bacillus subtilis. The structure determination process was an unusual one, involving 12 monomers of the enzyme in the asymmetric unit. This structure was solved by the multiple isomorphous replacement method with partial structure phase combination and molecular averaging. The final model, which includes 1380 residues and 522 water molecules in an asymmetric unit, has been refined at 1.9 Å and the current crystallographic R value is 0.201. The B. subtilis chorismate mutase is a homotrimer, with β-sheets from each monomer packing to form the core of a pseudo-αβ-barrel with helices on the outside of the trimer. In addition, the active sites have been located by using data from a complex with an endo-oxabicyclic inhibitor that mimics the transition state of the reaction. The structure of this complex has been refined to 2.2 Å with a current R value of 0.182 for a model that includes 1388 residues, 12 inhibitor molecules, and 530 water molecules in the asymmetric unit. In each trimer, three equivalent active sites are located at the interfaces of two adjacent summits.
KW - Claisen rearrangement
KW - Shikimate pathway
KW - X-ray crystallography
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U2 - 10.1073/pnas.90.18.8600
DO - 10.1073/pnas.90.18.8600
M3 - Article
C2 - 8378335
AN - SCOPUS:0027274818
SN - 0027-8424
VL - 90
SP - 8600
EP - 8603
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 18
ER -