1BRM

ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI

Summary for 1BRM

• Entry DOI: 10.2210/pdb1brm/pdb
• Descriptor: ASPARTATE-SEMIALDEHYDE DEHYDROGENASE (2 entities in total)
• Functional Keywords: dehydrogenase, escherichia coli, enzyme, nadp, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 3
• Total formula weight: 120170.21

Authors

Hadfield, A.T.,Kryger, G.,Ouyang, J.,Ringe, D.,Petsko, G.A.,Viola, R.E. (deposition date: 1998-08-24, release date: 1999-06-22, Last modification date: 2024-02-07)

Primary citation

Hadfield, A.,Kryger, G.,Ouyang, J.,Petsko, G.A.,Ringe, D.,Viola, R.
Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis.
J.Mol.Biol., 289:991-1002, 1999

PubMed Abstract: Aspartate beta-semialdehyde dehydrogenase (ASADH) lies at the first branch point in an essential aspartic biosynthetic pathway found in bacteria, fungi and the higher plants. Mutations in the asd gene encoding for ASADH that produce an inactive enzyme are lethal, which suggests that ASADH may be an effective target for antibacterial, herbicidal and fungicidal agents. We have solved the crystal structure of the Escherichia coli enzyme to 2.5 A resolution using single isomorphous replacement and 3-fold non-crystallographic symmetry. Each monomer has an N-terminal nucleotide-binding domain and a dimerisation domain. The presence of an essential cysteine locates the active site in a cleft between the two domains. The functional dimer has the appearance of a butterfly, with the NADP-binding domains forming the wings and the dimerisation domain forming the body.A histidine residue is identified as a likely acid/base catalyst in the enzymic reaction. Other amino acids implicated in the enzymic activity by mutagenesis are found in the active site region and define the substrate binding pocket.

PubMed: 10369777
DOI: 10.1006/jmbi.1999.2828

Experimental method

X-RAY DIFFRACTION (2.5 Å)