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Structure of dihydrodipicolinate synthase from Methanocaldococcus jannaschii.

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.

SUBMITTER: Padmanabhan B

PROVIDER: S-EPMC2802868 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature

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Structure of dihydrodipicolinate synthase from Methanocaldococcus jannaschii.

Padmanabhan Balasundaram B Strange Richard W RW Antonyuk Svetlana V SV Ellis Mark J MJ Hasnain S Samar SS Iino Hitoshi H Agari Yoshihiro Y Bessho Yoshitaka Y Yokoyama Shigeyuki S

Acta crystallographica. Section F, Structural biology and crystallization communications 20091127 Pt 12

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-repla ...[more]

PMID: 20054116

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