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Báo cáo khoa học: Cosubstrate-induced dynamics of D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida
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D-3-Hydroxybutyrate dehydrogenase fromPseudomonas putidabelongs to the family of short-chain dehydrogenases⁄reductases. We have determined X-ray structures of the D-3-hydroxybutyrate dehydrogenase fromPseudo-monas putida, which was recombinantly expressed in Escherichia coli,in three different crystal forms to resolutions between 1.9 and 2.1 A ˚ . | ỊFEBS Journal Cosubstrate-induced dynamics of D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida Karthik S. Paithankar1 Claudia Feller2 E. Bartholomeus Kuettner1 Antje Keim1 Marlis Grunow2 and Norbert Strater1 1 Center for Biotechnology and Biomedicine Institute of BioanalyticalChemistry Faculty of Chemistry and Mineralogy University of Leipzig Germany 2 Institute of Biochemistry Faculty of Biosciences Pharmacy and Psychology University of Leipzig Germany Keywords crystal structure loop closure protein dynamics SDR Correspondence M. Grunow Institute of Biochemistry Faculty of Biosciences Pharmacy and Psychology University of Leipzig BruderstraBe 34 D-04103 Leipzig Germany Fax 49 341 9736998 Tel 49 341 9736907 E-mail gru@rz.uni-leipzig.de N. Strater Center for Biotechnology and Biomedicine Institute of Bioanalytical Chemistry Faculty of Chemistry and Mineralogy University of Leipzig Deutscher Platz 5 D-04103 Leipzig Germany Fax 49 341 9731319 Tel 49 341 9731311 E-mail strater@bbz.uni-leipzig.de Received 5 July 2007 revised 8 August 2007 accepted 10 September 2007 doi 10.1111 j.1742-4658.2007.06102.x D-3-Hydroxybutyrate dehydrogenase from Pseudomonas putida belongs to the family of short-chain dehydrogenases reductases. We have determined X-ray structures of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida which was recombinantly expressed in Escherichia coli in three different crystal forms to resolutions between 1.9 and 2.1 A. The so-called substrate-binding loop residues 187-210 was partially disordered in several subunits in both the presence and absence of NAD . However in two subunits this loop was completely defined in an open conformation in the apoenzyme and in a closed conformation in the complex structure with NAD . Structural comparisons indicated that the loop moves as a rigid body by about 46 . However the two small a-helices aFG1 and aFG2 of the loop also re-orientated slightly during the conformational change. Probably the .