Structure of D-lactate dehydrogenase from Aquifex aeolicus complexed with NAD(+) and lactic acid (or pyruvate).
The crystal structure of D-lactate dehydrogenase from Aquifex aeolicus (aq_727) was determined to 2.12 A resolution in space group P2(1)2(1)2(1), with unit-cell parameters a = 90.94, b = 94.43, c = 188.85 A. The structure was solved by molecular replacement using the coenzyme-binding domain of Lactobacillus helveticus D-lactate dehydrogenase and contained two homodimers in the asymmetric unit. Each subunit of the homodimer was found to be in a ;closed' conformation with the NADH cofactor bound to the coenzyme-binding domain and with a lactate (or pyruvate) molecule bound at the interdomain active-site cleft.
Antonyuk
Svetlana V
SV
Molecular Biophysics Group, School of Biological Sciences, University of Liverpool, Crown Street, Liverpool L69 7ZB, England.
Strange
Richard W
RW
Ellis
Mark J
MJ
Bessho
Yoshitaka
Y
Kuramitsu
Seiki
S
Inoue
Yumiko
Y
Yokoyama
Shigeyuki
S
Hasnain
S Samar
SS
D001419:Bacteria / Q000201:enzymology* / Q000235:genetics; D020134:Catalytic Domain; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D005798:Genes, Bacterial; D045022:Lactate Dehydrogenases / Q000737:chemistry* / Q000235:genetics; D019344:Lactic Acid / Q000737:chemistry; D052198:Lactobacillus helveticus / Q000201:enzymology; D008958:Models, Molecular; D009243:NAD / Q000737:chemistry; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D019289:Pyruvic Acid / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D055672:Static Electricity
D021122:Protein Subunits; D011994:Recombinant Proteins; D009243:NAD; D019344:Lactic Acid; D019289:Pyruvic Acid; D045022:Lactate Dehydrogenases; C071195:D-lactate dehydrogenase