2YXG

Crystal structure of Dihyrodipicolinate Synthase (dapA)

Summary for 2YXG

• Entry DOI: 10.2210/pdb2yxg/pdb
• Descriptor: Dihydrodipicolinate synthase (2 entities in total)
• Functional Keywords: mj0244, dihydrodipicolinate synthase, tim beta/alpha-barrel fold, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, lyase
• Biological source: Methanocaldococcus jannaschii DSM 2661
• Cellular location: Cytoplasm (By similarity): Q57695
• Total number of polymer chains: 4
• Total formula weight: 126453.74

Authors

Padmanabhan, B.,Bessho, Y.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2007-04-26, release date: 2007-10-30, Last modification date: 2023-10-25)

Primary citation

Padmanabhan, B.,Strange, R.W.,Antonyuk, S.V.,Ellis, M.J.,Hasnain, S.S.,Iino, H.,Agari, Y.,Bessho, Y.,Yokoyama, S.
Structure of dihydrodipicolinate synthase from Methanocaldococcus jannaschii.
Acta Crystallogr.,Sect.F, 65:1222-1226, 2009

PubMed 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.

PubMed: 20054116
DOI: 10.1107/S174430910904651X

Experimental method

X-RAY DIFFRACTION (2.2 Å)