1ad1
From Proteopedia
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| - | [[Image:1ad1.jpg|left|200px]] | + | [[Image:1ad1.jpg|left|200px]] |
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| - | '''DIHYDROPTEROATE SYNTHETASE (APO FORM) FROM STAPHYLOCOCCUS AUREUS''' | + | {{Structure |
| + | |PDB= 1ad1 |SIZE=350|CAPTION= <scene name='initialview01'>1ad1</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Dihydropteroate_synthase Dihydropteroate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.15 2.5.1.15] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''DIHYDROPTEROATE SYNTHETASE (APO FORM) FROM STAPHYLOCOCCUS AUREUS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AD1 is a [ | + | 1AD1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AD1 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure and function of the dihydropteroate synthase from Staphylococcus aureus., Hampele IC, D'Arcy A, Dale GE, Kostrewa D, Nielsen J, Oefner C, Page MG, Schonfeld HJ, Stuber D, Then RL, J Mol Biol. 1997 Apr 25;268(1):21-30. PMID:[http:// | + | Structure and function of the dihydropteroate synthase from Staphylococcus aureus., Hampele IC, D'Arcy A, Dale GE, Kostrewa D, Nielsen J, Oefner C, Page MG, Schonfeld HJ, Stuber D, Then RL, J Mol Biol. 1997 Apr 25;268(1):21-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9149138 9149138] |
[[Category: Dihydropteroate synthase]] | [[Category: Dihydropteroate synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: apo form]] | [[Category: apo form]] | ||
[[Category: complex with oh-ch2-pterin-pyrophosphate]] | [[Category: complex with oh-ch2-pterin-pyrophosphate]] | ||
| - | [[Category: | + | [[Category: dhp]] |
[[Category: dihydropteroate synthetase]] | [[Category: dihydropteroate synthetase]] | ||
[[Category: synthetase]] | [[Category: synthetase]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''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 09:55:56 2008'' |
Revision as of 07:56, 20 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Dihydropteroate synthase, with EC number 2.5.1.15 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DIHYDROPTEROATE SYNTHETASE (APO FORM) FROM STAPHYLOCOCCUS AUREUS
Overview
The gene encoding the dihydropteroate synthase of staphylococcus aureus has been cloned, sequenced and expressed in Escherichia coli. The protein has been purified for biochemical characterization and X-ray crystallographic studies. The enzyme is a dimer in solution, has a steady state kinetic mechanism that suggests random binding of the two substrates and half-site reactivity. The crystal structure of apo-enzyme and a binary complex with the substrate analogue hydroxymethylpterin pyrophosphate were determined at 2.2 A and 2.4 A resolution, respectively. The enzyme belongs to the group of "TIM-barrel" proteins and crystallizes as a non-crystallographic dimer. Only one molecule of the substrate analogue bound per dimer in the crystal. Sequencing of nine sulfonamide-resistant clinical isolates has shown that as many as 14 residues could be involved in resistance development. The residues are distributed over the surface of the protein, which defies a simple interpretation of their roles in resistance. Nevertheless, the three-dimensional structure of the substrate analogue binary complex could give important insight into the molecular mechanism of this enzyme.
About this Structure
1AD1 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Structure and function of the dihydropteroate synthase from Staphylococcus aureus., Hampele IC, D'Arcy A, Dale GE, Kostrewa D, Nielsen J, Oefner C, Page MG, Schonfeld HJ, Stuber D, Then RL, J Mol Biol. 1997 Apr 25;268(1):21-30. PMID:9149138
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