1gl3
From Proteopedia
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| - | [[Image:1gl3.gif|left|200px]] | + | [[Image:1gl3.gif|left|200px]] |
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| - | '''ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE IN COMPLEX WITH NADP AND SUBSTRATE ANALOGUE S-METHYL CYSTEINE SULFOXIDE''' | + | {{Structure |
| + | |PDB= 1gl3 |SIZE=350|CAPTION= <scene name='initialview01'>1gl3</scene>, resolution 2.6Å | ||
| + | |SITE= <scene name='pdbsite=AT1:Ndp+Binding+Site+For+Chain+B'>AT1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene> and <scene name='pdbligand=NDP:NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NDP</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE IN COMPLEX WITH NADP AND SUBSTRATE ANALOGUE S-METHYL CYSTEINE SULFOXIDE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GL3 is a [ | + | 1GL3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL3 OCA]. |
==Reference== | ==Reference== | ||
| - | Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase., Hadfield A, Shammas C, Kryger G, Ringe D, Petsko GA, Ouyang J, Viola RE, Biochemistry. 2001 Dec 4;40(48):14475-83. PMID:[http:// | + | Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase., Hadfield A, Shammas C, Kryger G, Ringe D, Petsko GA, Ouyang J, Viola RE, Biochemistry. 2001 Dec 4;40(48):14475-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11724560 11724560] |
[[Category: Aspartate-semialdehyde dehydrogenase]] | [[Category: Aspartate-semialdehyde dehydrogenase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:24:36 2008'' |
Revision as of 09:24, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Aspartate-semialdehyde dehydrogenase, with EC number 1.2.1.11 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE IN COMPLEX WITH NADP AND SUBSTRATE ANALOGUE S-METHYL CYSTEINE SULFOXIDE
Overview
Aspartate-beta-semialdehyde dehydrogenase (ASADH) lies at the first branch point in the biosynthetic pathway through which bacteria, fungi, and the higher plants synthesize amino acids, including lysine and methionine and the cell wall component diaminopimelate from aspartate. Blocks in this biosynthetic pathway, which is absent in mammals, are lethal, and inhibitors of ASADH may therefore serve as useful antibacterial, fungicidal, or herbicidal agents. We have determined the structure of ASADH from Escherichia coli by crystallography in the presence of its coenzyme and a substrate analogue that acts as a covalent inhibitor. This structure is comparable to that of the covalent intermediate that forms during the reaction catalyzed by ASADH. The key catalytic residues are confirmed as cysteine 135, which is covalently linked to the intermediate during the reaction, and histidine 274, which acts as an acid/base catalyst. The substrate and coenzyme binding residues are also identified, and these active site residues are conserved throughout all of the ASADH sequences. Comparison of the previously determined apo-enzyme structure [Hadfield et al. J. Mol. Biol. (1999) 289, 991-1002] and the complex presented here reveals a conformational change that occurs on binding of NADP that creates a binding site for the amino acid substrate. These results provide a structural explanation for the preferred order of substrate binding that is observed kinetically.
About this Structure
1GL3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase., Hadfield A, Shammas C, Kryger G, Ringe D, Petsko GA, Ouyang J, Viola RE, Biochemistry. 2001 Dec 4;40(48):14475-83. PMID:11724560
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