1brm: Difference between revisions
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==Overview== | ==Overview== | ||
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, . | 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. | ||
==About this Structure== | ==About this Structure== | ||
1BRM is a | 1BRM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Aspartate-semialdehyde_dehydrogenase Aspartate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.11 1.2.1.11] Structure known Active Sites: AT1, AT2 and AT3. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BRM OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: nadp]] | [[Category: nadp]] | ||
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Revision as of 16:23, 5 November 2007
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ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI
OverviewOverview
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.
About this StructureAbout this Structure
1BRM is a Single protein structure of sequence from Escherichia coli. Active as Aspartate-semialdehyde dehydrogenase, with EC number 1.2.1.11 Structure known Active Sites: AT1, AT2 and AT3. Full crystallographic information is available from OCA.
ReferenceReference
Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis., Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R, J Mol Biol. 1999 Jun 18;289(4):991-1002. PMID:10369777
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