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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 12(65), p. 1209-1213, 2009

DOI: 10.1107/s1744309109044935

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Structure ofD-lactate dehydrogenase fromAquifex aeolicuscomplexed with NAD+and lactic acid (or pyruvate)

Journal article published in 2009 by Svetlana V. Antonyuk ORCID, Richard W. Strange, Mark J. Ellis, Yoshitaka Bessho, Seiki Kuramitsu, Yumiko Inoue, Shigeyuki Yokoyama, S. Samar Hasnain
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

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.