1dam
From Proteopedia
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| - | [[Image:1dam.jpg|left|200px]] | + | [[Image:1dam.jpg|left|200px]] |
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| - | '''DETHIOBIOTIN SYNTHETASE COMPLEXED WITH DETHIOBIOTIN, ADP, INORGANIC PHOSPHATE AND MAGNESIUM''' | + | {{Structure |
| + | |PDB= 1dam |SIZE=350|CAPTION= <scene name='initialview01'>1dam</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=DTB:6-(5-METHYL-2-OXO-IMIDAZOLIDIN-4-YL)-HEXANOIC ACID'>DTB</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Dethiobiotin_synthase Dethiobiotin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.3.3 6.3.3.3] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''DETHIOBIOTIN SYNTHETASE COMPLEXED WITH DETHIOBIOTIN, ADP, INORGANIC PHOSPHATE AND MAGNESIUM''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DAM is a [ | + | 1DAM 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=1DAM OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of two quaternary complexes of dethiobiotin synthetase, enzyme-MgADP-AlF3-diaminopelargonic acid and enzyme-MgADP-dethiobiotin-phosphate; implications for catalysis., Kack H, Sandmark J, Gibson KJ, Schneider G, Lindqvist Y, Protein Sci. 1998 Dec;7(12):2560-6. PMID:[http:// | + | Crystal structure of two quaternary complexes of dethiobiotin synthetase, enzyme-MgADP-AlF3-diaminopelargonic acid and enzyme-MgADP-dethiobiotin-phosphate; implications for catalysis., Kack H, Sandmark J, Gibson KJ, Schneider G, Lindqvist Y, Protein Sci. 1998 Dec;7(12):2560-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9865950 9865950] |
[[Category: Dethiobiotin synthase]] | [[Category: Dethiobiotin synthase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: phosphoryl transfer]] | [[Category: phosphoryl transfer]] | ||
| - | ''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 10:35:25 2008'' |
Revision as of 08:35, 20 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | , , and | ||||||
| Activity: | Dethiobiotin synthase, with EC number 6.3.3.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DETHIOBIOTIN SYNTHETASE COMPLEXED WITH DETHIOBIOTIN, ADP, INORGANIC PHOSPHATE AND MAGNESIUM
Overview
The crystal structures of two complexes of dethiobiotin synthetase, enzyme-diaminopelargonic acid-MgADP-AlF3 and enzyme-dethiobiotin-MgADP-Pi, respectively, have been determined to 1.8 A resolution. In dethiobiotin synthetase, AlF3 together with carbamylated diaminopelargonic acid mimics the phosphorylated reaction intermediate rather than the transition state complex for phosphoryl transfer. Observed differences in the binding of substrate, diaminopelargonic acid, and the product, dethiobiotin, suggest considerable displacements of substrate atoms during the ring closure step of the catalytic reaction. In both complexes, two metal ions are observed at the active site, providing evidence for a two-metal mechanism for this enzyme.
About this Structure
1DAM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of two quaternary complexes of dethiobiotin synthetase, enzyme-MgADP-AlF3-diaminopelargonic acid and enzyme-MgADP-dethiobiotin-phosphate; implications for catalysis., Kack H, Sandmark J, Gibson KJ, Schneider G, Lindqvist Y, Protein Sci. 1998 Dec;7(12):2560-6. PMID:9865950
Page seeded by OCA on Thu Mar 20 10:35:25 2008
Categories: Dethiobiotin synthase | Escherichia coli | Single protein | Gibson, K J. | Kaeck, H. | Lindqvist, Y. | Sandmark, J. | Schneider, G. | ADP | DTB | MG | PO4 | Atp-binding | Biotin biosynthesis | Ligase | Magnesium | Phosphoryl transfer
