Structure of Escherichia coli malate dehydrogenase at 1.45 A resolution.
The structure of apo malate dehydrogenase from Escherichia coli has been determined to 1.45 A resolution. The crystals belonged to space group C2, with unit-cell parameters a = 146.0, b = 52.0, c = 168.9 A, beta = 102.2 degrees. The structure was determined with the molecular-replacement pipeline program BALBES and was refined to a final R factor of 18.6% (R(free) = 21.4%). The final model has two dimers in the asymmetric unit. In each dimer one monomer contains the active-site loop in the open conformation, whereas in the opposing monomer the active-site loop is disordered.
Zaitseva
Jelena
J
Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, USA.
Meneely
Kathleen M
KM
Lamb
Audrey L
AL
D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D008291:Malate Dehydrogenase / Q000737:chemistry*; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D055672:Static Electricity
D008291:Malate Dehydrogenase