1brm: Difference between revisions
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==Overview== | ==Overview== | ||
Aspartate beta-semialdehyde dehydrogenase (ASADH) lies at the first branch | 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== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hadfield, A | [[Category: Hadfield, A T.]] | ||
[[Category: Kryger, G.]] | [[Category: Kryger, G.]] | ||
[[Category: Ouyang, J.]] | [[Category: Ouyang, J.]] | ||
[[Category: Petsko, G | [[Category: Petsko, G A.]] | ||
[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
[[Category: Viola, R | [[Category: Viola, R E.]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
[[Category: dehydrogenase]] | [[Category: dehydrogenase]] | ||
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[[Category: nadp]] | [[Category: nadp]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:22 2008'' | ||
Revision as of 12:58, 21 February 2008
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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 Known structural/functional Sites: , and . 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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