1brm: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1brm. | [[Image:1brm.jpg|left|200px]]<br /><applet load="1brm" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1brm" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1brm, resolution 2.5Å" /> | caption="1brm, resolution 2.5Å" /> | ||
'''ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI'''<br /> | '''ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
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] | 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] Known structural/functional Sites: <scene name='pdbsite=AT1:Active Site Identified From Modified CYS. Site Site_iden ...'>AT1</scene>, <scene name='pdbsite=AT2:Active Site Identified From Modified CYS. Site Site_iden ...'>AT2</scene> and <scene name='pdbsite=AT3:Active Site Identified From Modified CYS'>AT3</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BRM OCA]. | ||
==Reference== | ==Reference== | ||
| Line 27: | Line 26: | ||
[[Category: nadp]] | [[Category: nadp]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:32:11 2007'' | ||
Revision as of 15:22, 18 December 2007
|
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
Page seeded by OCA on Tue Dec 18 14:32:11 2007