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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 12(65), p. 1222-1226, 2009

DOI: 10.1107/s174430910904651x

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Structure of dihydrodipicolinate synthase fromMethanocaldococcus jannaschii

Journal article published in 2009 by Balasundaram Padmanabhan, Richard W. Strange, Svetlana V. Antonyuk ORCID, Mark J. Ellis, S. Samar Hasnain, Hitoshi Iino, Yoshihiro Agari, Yoshitaka Bessho, Shigeyuki Yokoyama
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

In bacteria and plants, dihydrodipicolinate synthase (DHDPS) plays a key role in the (S)-lysine biosynthesis pathway. DHDPS catalyzes the first step of the condensation of (S)-aspartate-beta-semialdehyde and pyruvate to form an unstable compound, (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid. The activity of DHDPS is allosterically regulated by (S)-lysine, a feedback inhibitor. The crystal structure of DHDPS from Methanocaldococcus jannaschii (MjDHDPS) was solved by the molecular-replacement method and was refined to 2.2 A resolution. The structure revealed that MjDHDPS forms a functional homotetramer, as also observed in Escherichia coli DHDPS, Thermotoga maritima DHDPS and Bacillus anthracis DHDPS. The binding-site region of MjDHDPS is essentially similar to those found in other known DHDPS structures.